Persius/hicric huggingface dataset:
RAB23
Ras-related protein Rab-23 is a protein that in humans is encoded by the RAB23 gene. Alternative splicing occurs at this gene locus and two transcript variants encoding the same protein have been identified.

# Function
RAB23 belongs to the small GTPase superfamily, Rab family. It may be involved in small GTPase mediated signal transduction and intracellular protein transportation.
RAB23 is an essential negative regulator of the Sonic hedgehog signaling pathway.  The first understanding of biological processes requiring the Rab23 gene came from 2 independent  mouse mutations in the gene   and an epistasis analysis with mutations in the mouse shh gene. These studies showed that the gene is required for normal development of the brain and spinal cord and that the morphological defects seen in mutant embryos, such as failure to close dorsal regions of the neural tube during development, appeared secondary to expansion of ventral and reduction of dorsal identities in the developing neural tube.  These same mutations implicated the RAB23 gene in development of digits and eyes.  The mouse open brain (opb) and Sonic hedgehog (Shh) genes have opposing roles in neural patterning: opb is required for dorsal cell types and Shh is required for ventral cell types in the spinal cord.
RAB27
Rab27 is a member of the Rab subfamily of GTPases. Rab27 is post translationally modified by the addition of two geranylgeranyl groups on the two C-terminal cysteines.

# Pathology
Mutations that prevent the expression of Rab27 ('knock out' mutations) cause the hypopigmentation and immunodefficiency disorder known as type II Griscelli syndrome, while a decrease in Rab27 prenylation is thought to be involved in choroideremia.
The symptoms of type II Griscelli syndrome have shown that Rab27 is involved in melanosome transport in melanocytes and in cytotoxic killing activity in cytotoxic T lymphoblasts. In melanocytes Rab27 binds the melanosome. The melanosome is transported along the microtubule. Rab27 then recruits Slac2A and myosin Va, these enzymes are essential for the transfer of the melanosomes from the microtubules to actin filaments. The melanosomes can now continue on their path towards the cell periphery. If either Rab27, Slac2A or myosin Va are absent then the melansomes remain in the perinuclear region of the cell. This disruption in pigmentation results in the hypopigmentation seen in the silvery hair colour of patients with Griscelli syndrome.
RAD18
E3 ubiquitin-protein ligase RAD18 is an enzyme that in humans is encoded by the RAD18 gene.

# Function
The protein encoded by this gene is highly similar to S. cerevisiae DNA damage repair protein Rad18. Yeast Rad18 functions through its interaction with Rad6, which is a ubiquitin-conjugating enzyme required for post-replication repair of damaged DNA. Similar to its yeast counterpart, this protein is able to interact with the human homolog of yeast Rad6 protein through a conserved ring finger motif.  Mutation of this motif results in defective replication of UV-damaged DNA and hypersensitivity to multiple mutagens.

# Animal models
Model organisms have been used in the study of RAD18 function. A conditional knockout mouse line, called Rad18tm1a(EUCOMM)Wtsi, was generated as part of the EUCOMM program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists  at the Wellcome Trust Sanger Institute. Mice lacking Rad18 had no significant defects in viability or fertility, therefore  male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.
Twenty five tests were carried out and four significant phenotypes were reported:
- Mutant male mice had a decreased body weight compared to wildtype control mice.
- Mutant male mice showed increased activity, VO2 and energy expenditure, determined by indirect calorimetry.
- Dual-energy X-ray absorptiometry (DEXA) showed mutant male mice had a decrease in fat mass.
- A micronucleus test found a potential increase in DNA damage in mutant mice.
A knockout in a human colorectal cancer cell line, HCT116, has also been created.

# Interactions
RAD18 has been shown to interact with HLTF, UBE2B and UBE2A.
RAPSN
43 kDa receptor-associated protein of the synapse (rapsyn) is a protein that in humans is encoded by the RAPSN gene.

# Function
This protein belongs to a family of proteins that are receptor associated proteins of the synapse. It contains a conserved cAMP-dependent protein kinase phosphorylation site. It is believed to play some role in anchoring or stabilizing the nicotinic acetylcholine receptor at synaptic sites. It may link the receptor to the underlying postsynaptic cytoskeleton, possibly by direct association with actin or spectrin. Two splice variants have been identified for this gene.

# Role in health and disease
In the neuromuscular junction there is a vital pathway that maintains synaptic structure and results in the aggregation and localization of the acetylcholine receptor (AChR) on the postsynaptic folds. This pathway consists of agrin, muscle-specific tyrosine kinase (MuSK protein), AChRs and the AChR-clustering protein rapsyn, encoded by RAPSN. Genetic mutations of the proteins in the neuromuscular junction are associated with Congenital myasthenic syndrome (CMS). Postsynaptic defects are the most frequent cause of CMS and often result in abnormalities in the acetylcholine receptor. The vast majority of mutations causing CMS are found in the AChR subunits and rapsyn genes.
The rapsyn protein interacts directly with the AChRs and plays a vital role in agrin-induced clustering of the AChR. Without rapsyn, functional synapses cannot be created as the folds do not form properly. Patients with CMS-related mutations of the rapsyn protein typically are either homozygous for N88K or heterozygous for N88K and a second mutation. The major effect of the mutation N88K in rapsyn is to reduce the stability of AChR clusters. The second mutation can be a determining factor in the severity of the disease.
Studies have shown that most patients with CMS that have rapsyn mutations carry the common mutation N88K on at least one allele. However, research has revealed that there is a small population of patients who do not carry the N88K mutation on either of their alleles, but instead have different mutations of the RAPSN gene on both of their alleles. Two novel missense mutations that have been found are R164C and L283P and the result is a decrease in co-clustering of AChR with raspyn. A third mutation is the intronic base alteration IVS1-15C>A and it causes abnormal splicing of RAPSN RNA. These results show that diagnostic screening for CMS mutations of the RAPSN gene cannot be based exclusively on the detection of N88K mutations

# Interactions
RAPSN has been shown to interact with KHDRBS1.
RBBP4
Histone-binding protein RBBP4 (also known as RbAp48, or NURF55) is a protein that in humans is encoded by the RBBP4 gene.

# Function
This gene encodes a ubiquitously expressed nuclear protein that belongs to a highly conserved subfamily of WD-repeat proteins. It is present in protein complexes involved in histone acetylation and chromatin assembly. It is part of the Mi-2/NuRD complex that has been implicated in chromatin remodeling and transcriptional repression associated with histone deacetylation. This encoded protein is also part of corepressor complexes, which is an integral component of transcriptional silencing. It is found among several cellular proteins that bind directly to retinoblastoma protein to regulate cell proliferation. This protein also seems to be involved in transcriptional repression of E2F-responsive genes.

# Clinical significance
A decrease of RbAp48 in the dentate gyrus (DG) of the hippocampus in the brain is suspected to be a main cause of memory loss in normal aging.  An age related decrease in RbAp48 is observed in the DG from human post-mortem tissue and also in mice.  Furthermore, a gene knockin of a dominant negative form of RbAp48 of causes memory deficits in young mice similar to that observed in older mice. Finally lentiviral gene transfer to increase the expression of RbAp48 in the brain reverses memory deficits in older mice.
RBBP4 works at least in part through the PKA-CREB1-CPB pathway. Hence one possible therapeutic approach to restore age-related memory loss is the use of PKA-CREB1-CPB pathway stimulating drugs. It has previously been shown that dopamine D1/D5 agonists such as 6-Br-APB and SKF-38,393 that are positively coupled to adenylyl cyclase and the cAMP phosphodieserase inhibitor rolipram reduce memory defects in aged mice.

# Interactions
RBBP4 has been shown to interact with:
- BRCA1,
- CREBBP,
- GATAD2B,
- HDAC1,
- HDAC2,
- HDAC3,
- MTA2,
- RB,
- SAP30,  and
- SIN3A.
RBBP6
Retinoblastoma-binding protein 6 is a protein that in humans is encoded by the RBBP6 gene.

# Function
The retinoblastoma tumor suppressor (pRB) protein binds with many other proteins. In various human cancers, pRB suppresses cellular proliferation and is inactivated. Cell cycle-dependent phosphorylation regulates the activity of pRB. This gene encodes a protein which binds to underphosphorylated but not phosphorylated pRB. Multiple alternatively spliced transcript variants that encode different isoforms have been found for this gene.

# Interactions
RBBP6 has been shown to interact with Y box binding protein 1.
RBBP7
Histone-binding protein RBBP7 is a protein that in humans is encoded by the RBBP7 gene.

# Function
This protein is a ubiquitously expressed nuclear protein and belongs to a highly conserved subfamily of WD-repeat proteins. It is found among several proteins that binds directly to retinoblastoma protein, which regulates cell proliferation. The encoded protein is found in many histone deacetylase complexes, including mSin3 co-repressor complex. It is also present in protein complexes involved in chromatin assembly. This protein can interact with BRCA1 tumor-suppressor gene and may have a role in the regulation of cell proliferation and differentiation.

# Model organisms
Model organisms have been used in the study of RBBP7 function. A conditional knockout mouse line, called Rbbp7tm1a(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 one tests were carried out on mutant mice and one significant abnormality was observed: hemizygous mutant males had decreased CD4-positive and CD8-positive T cell numbers.

# Interactions
RBBP7 has been shown to interact with:
- BRCA1,
- GATAD2B,
- HDAC1,
- MTA2,
- Retinoblastoma protein,
- SAP30,  and
- SIN3A.
RBCK1
RanBP-type and C3HC4-type zinc finger-containing protein 1 is a protein that in humans is encoded by the RBCK1 gene.
The protein encoded by this gene is similar to mouse UIP28/UbcM4 interacting protein. Alternative splicing has been observed at this locus, resulting in distinct isoforms.

# Clinical significance
A family quartet was found with two children, both affected with a previously unreported disease, characterized by progressive muscular weakness and cardiomyopathy, with normal intelligence. During the course of the study, one additional unrelated patient was found with a comparable phenotype. From whole-genome sequence data,  RBCK1, a gene encoding an E3 ubiquitin-protein ligase, was identified as the most likely candidate gene, with two protein-truncating mutations in probands in the first family. Sanger sequencing identified a private homozygous splice variant in RBCK1 in the proband in the second family, yet SNP genotyping revealed a 1.2Mb copy-neutral region of homozygosity covering RBCK1. RNA-Seq confirmed aberrant splicing of RBCK1 transcripts, resulting in truncated protein products. Ten other individuals with mutations in RBCK1 and overlapping phenotypes have been identified.
RBM39
RNA-binding protein 39 is a protein that in humans is encoded by the RBM39 gene.

# Function
The protein encoded by this gene is an RNA binding protein and possible splicing factor. The encoded protein is found in the nucleus, where it colocalizes with core spliceosomal proteins. Studies of a mouse protein with high sequence similarity to this protein suggest that this protein may act as a transcriptional coactivator for JUN/AP-1 and estrogen receptors. Multiple transcript variants encoding different isoforms have been observed for this gene.

# Interactions
RBM39 has been shown to interact with Estrogen receptor alpha, Estrogen receptor beta and C-jun.
RBM8A
RNA-binding protein 8A is a protein that in humans is encoded by the RBM8A gene.
This gene encodes a protein with a conserved RNA-binding motif. The protein is found predominantly in the nucleus, although it is also present in the cytoplasm. It is preferentially associated with mRNAs produced by splicing, including both nuclear mRNAs and newly exported cytoplasmic mRNAs. It is thought that the protein remains associated with spliced mRNAs as a tag to indicate where introns had been present, thus coupling pre- and post-mRNA splicing events. Previously, it was thought that two genes encode this protein, RBM8A and RBM8B; it is now thought that the RBM8B locus is a pseudogene. Two alternative start codons result in two forms of the protein, and this gene also uses multiple polyadenylation sites.

# Interactions
RBM8A has been shown to interact with IPO13, MAGOH and UPF3A.

# Related gene problems
- TAR syndrome
- 1q21.1 deletion syndrome
- 1q21.1 duplication syndrome
RBMS1
RNA-binding motif, single-stranded-interacting protein 1 is a protein that in humans is encoded by the RBMS1 gene.

# Function
This gene encodes a member of a small family of proteins which bind single stranded DNA/RNA. These proteins are characterized by the presence of two sets of ribonucleoprotein consensus sequence (RNP-CS) that contain conserved motifs, RNP1 and RNP2, originally described in RNA binding proteins, and required for DNA binding. These proteins have been implicated in such diverse functions as DNA replication, gene transcription, cell cycle progression and apoptosis. Multiple transcript variants, resulting from alternative splicing and encoding different isoforms, have been described. Several of these were isolated by virtue of their binding to either strand of an upstream element of c-myc (MSSPs), or by phenotypic complementation of cdc2 and cdc13 mutants of yeast (scr2), or as a potential human repressor of HIV-1 and ILR-2 alpha promoter transcription (YC1). A pseudogene for this locus is found on chromosome 12.

# Interactions
RBMS1 has been shown to interact with Polymerase (DNA directed), alpha 1.
RBPMS
RNA-binding protein with multiple splicing is a protein that in humans is encoded by the RBPMS gene.

# Function
This gene encodes a member of the RRM family of RNA-binding proteins. The RRM domain is between 80-100 amino acids in length and family members contain one to four copies of the domain. The RRM domain consists of two short stretches of conserved sequence called RNP1 and RNP2, as well as a few highly conserved hydrophobic residues. The protein encoded by this gene has a single, putative RRM domain in its N-terminus. Alternative splicing results in multiple transcript variants encoding different isoforms.
It is uniquely expressed in retinal ganglion cells in the mammalian retina, for reasons unknown.

# Interactions
RBPMS has been shown to interact with SMUG1.
RCHY1
RING finger and CHY zinc finger domain-containing protein 1 is a protein that in humans is encoded by the RCHY1 gene.

# Function
The protein encoded by this gene has ubiquitin-protein ligase activity. This protein binds with p53 and promotes the ubiquitin-mediated proteosomal degradation of p53. This gene is oncogenic because loss of p53 function contributes directly to malignant tumor development. Transcription of this gene is regulated by p53. Alternative splicing results in multiple transcript variants encoding different isoforms.

# Interactions
RCHY1 has been shown to interact with P53 and Androgen receptor.
RDH11
Retinol dehydrogenase 11 is an enzyme that in humans is encoded by the RDH11 gene.
RHD11, a member of the short-chain dehydrogenase/reductase (SDR) superfamily of oxidoreductases, is expressed at high levels in prostate epithelium, and its expression is regulated by androgens.

# Clinical significance
Mutations in RDH11 are associated to                 retinitis pigmentosa            .
RDH13
Retinol dehydrogenase 13 (all-trans/9-cis) is a protein that in humans is encoded by the RDH13 gene. This gene encodes a mitochondrial short-chain dehydrogenase/reductase, which catalyzes the reduction and oxidation of retinoids. The encoded enzyme may function in retinoic acid production and may also protect the mitochondria against oxidative stress. Alternatively spliced transcript variants have been described.

# Gene
The human RDH13 gene is on the 19th chromosome, with its specific localization being 19q13.42. The gene contains 12 exons in total.

# Structure
The analysis of the submitochondrial localization of RDH13 indicates its association with the inner mitochondrial membrane. The primary structure of RDH13 contains two hydrophobic segments, 221 and 242261, which are sufficiently long to serve as transmembrane segments; however, as shown in the present study, alkaline extraction completely removes the protein from the membrane, indicating that RDH13 is a peripheral membrane protein. The peripheral association of RDH13 with the membrane further distinguishes this protein from the microsomal retinaldehyde reductases, which are integral membrane proteins that appear to be anchored in the membrane via their N-terminal hydrophobic segments.

# Function
RDH13 is most closely related to the NADP+-dependent microsomal enzymes RDH11, RDH12 and RDH14. Purified RDH13 acts on retinoids in an oxidative reductive manner, and strongly prefers the cofactor NADPH over NADH. Moreover, RDH13 is much has much more efficient reductase activity than dehydrogenase activity. RDH13 as a retinaldehyde reductase is significantly less active than that of a related protein RDH11, primarily because of the much higher Km value for retinaldehyde. However, the kcat value of RDH13 for retinaldehyde reduction. arable with that of RDH11, and the Km values of the two enzymes for NADPH are also very similar. Thus, consistent with its sequence similarity to RDH11, RDH12 and RDH14, RDH13 acts as an NADP+-dependent retinaldehyde reductase.
RDH13 is localized in the mitochondria, which is different from the other members of this family, as they localize to the endoplasmic reticulum. The exact sequence targeting RDH13 to the mitochondria remains to be established.

# Clinical significance
RDH13 is part of a subfamily of four retinol dehydrogenases, RDH11, RDH12, RDH13, and RDH14, that display dual-substrate specificity, uniquely metabolizing all-trans- and cis-retinols with C(15) pro-R specificity. The metabolites involved in these reactions are known as retinoids, which are chromophores involved in vision, transcriptional regulation, and cellular differentiation. RDH11-14 could be involved in the first step of all-trans- and 9-cis-retinoic acid production in many tissues. RDH11-14 fill the gap in our understanding of 11-cis-retinal and all-trans-retinal transformations in photoreceptor and retinal pigment epithelial cells. The dual-substrate specificity of this subfamily explains the minor phenotype associated with mutations in 11-cis-retinol dehydrogenase (RDH5) causing fundus albipunctatus in humans.
RECQL
ATP-dependent DNA helicase Q1 is an enzyme that in humans is encoded by the RECQL gene.
The protein encoded by this gene is a member of the RecQ DNA helicase family. DNA helicases are enzymes involved in various types of DNA repair, including mismatch repair, nucleotide excision repair and direct repair. Some members of this family are associated with genetic disorders with predisposition to malignancy and chromosomal instability. The biological function of this helicase has not yet been determined. Two alternatively spliced transcripts, which encode the same isoform but differ in their 5' and 3' UTRs, have been described.

# Interactions
RECQL has been shown to interact with KPNA4 and Karyopherin alpha 2.
REEP2
Receptor expression-enhancing protein 2 is a protein that in humans is encoded by the REEP2 gene.

# Function
The protein encoded by REEP2 belongs to a family of proteins with receptor enhancing expression capabilities, including possible enhancement of G protein-coupled receptors. The REEP2 protein shows a restricted mode of expression in human tissues .

# Clinical significance
REEP2 mutations have been reported in families with hereditary spastic paraplegia.
REG3A
Regenerating islet-derived protein 3 alpha (or Regenerating islet-derived protein III-alpha) formerly known as HIP/PAP (Hepatocarcinoma-Intestine-Pancreas/Pancreatitis-Associated Protein) and peptide 23 is a protein that in humans is encoded by the REG3A gene.
This gene encodes a pancreatic secretory protein that may be involved in cell proliferation or differentiation. It has similarity to the C-type lectin superfamily. The enhanced expression of this gene is observed during pancreatic inflammation and liver carcinogenesis. Multiple alternatively spliced transcript variants encoding the same protein have been described for this gene but the full length nature of some transcripts is not yet known.
Reg3A (UniProt Q0614 1) is a bactericidal C-type lectin that is constitutively produced in the intestine that has antibacterial properties against Gram-positive bacteria. Bacterial killing is mediated by binding to surface-exposed carbohydrate moieties of bacterial peptidoglycan.
REPS2
RalBP1-associated Eps domain-containing protein 2 is a protein that in humans is encoded by the REPS2 gene.

# Function
The product of this gene is part of a protein complex that regulates the endocytosis of growth factor receptors. The encoded protein directly interacts with a GTPase activating protein that functions downstream of the small G protein Ral. Its expression can negatively affect receptor internalization and inhibit growth factor signaling. Multiple transcript variants encoding different isoforms have been found for this gene.

# Interactions
REPS2 has been shown to interact with EPN1, EPS15 and RALBP1.
RGS13
Regulator of G-protein signaling 13 is a protein that in humans is encoded by the RGS13 gene.
RGS 13 is a member of R4 subfamily of RGS (Regulators of G Protein Signaling) proteins which have only short peptide sequences flanking the RGS domain. RGS 13 suppresses the immunoglobulin E- mediated allergic responses.
The protein encoded by this gene is a member of the regulator of G protein signaling (RGS) family. RGS family members share similarity with S. cerevisiae SST2 and C. elegans egl-10 proteins, which contain a characteristic conserved RGS domain. RGS proteins accelerate GTPase activity of G protein alpha-subunits, thereby driving G protein into their inactive GDP-bound form, thus negatively regulating G protein signaling. RGS proteins have been implicated in the fine tuning of a variety of cellular events in response to G protein-coupled receptor activation. The biological function of this gene, however, is unknown. Two transcript variants encoding the same isoform exist.