Persius/hicric huggingface dataset:
CRLF1
Cytokine receptor-like factor 1 is a protein that in humans is encoded by the CRLF1 gene.

# Function
This gene encodes a member of the cytokine type I receptor family. The protein forms a secreted complex with cardiotrophin-like cytokine factor 1 and acts on cells expressing ciliary neurotrophic factor receptors. The complex can promote survival of neuronal cells.

# Clinical significance
Mutations in this gene are associated with two conditions, both rare:
- Cold-induced sweating syndrome, characterized by profuse hyperhidrosis in cold environmental temperature and characteristic craniofacial and skeletal features)
- Crisponi syndrome (CS), characterized by neonatal-onset paroxysmal muscular contractions, abnormal function of the autonomic nervous system and craniofacial and skeletal manifestations such as thick and arched eyebrows, a short nose with anteverted nostrils, full cheeks, an inverted upper lip and a small mouth.
It is unknown whether the two conditions are distinct clinical entities or a single clinical entity with variable expressions.
Other characteristic features in CRLF1 mutation include marfanoid habitus with progressive kyphoscoliosis and craniofacial characteristics including dolichocephaly, a slender face with poor expression, a nose with hypoplastic nares, malar hypoplasia and prognathism.
CRMP1
Collapsin response mediator protein 1, encoded by the CRMP1 gene, is a human protein of the CRMP family.
This gene encodes a member of a family of cytosolic phosphoproteins expressed exclusively in the nervous system. The encoded protein is thought to be a part of the semaphorin signal transduction pathway implicated in semaphorin-induced growth cone collapse during neural development. Alternative splicing results in multiple transcript variants.
CRMP1 mediates reelin signaling in cortical neuronal migration. Mice deficient in CRMP1 exhibit impaired long-term potentiation and impaired spatial learning and memory.
CRMP1 gene overlaps with another gene called EVC.

# Interactions
CRMP1 has been shown to interact with DPYSL2.
CRSP3
Mediator of RNA polymerase II transcription subunit 23 is an enzyme that in humans is encoded by the MED23 gene.

# Function
The activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The protein encoded by this gene is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. This protein also acts as a metastasis suppressor. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.

# Interactions
CRSP3 has been shown to interact with Estrogen receptor alpha, CEBPB and Cyclin-dependent kinase 8.
CRTC1
CREB-regulated transcription coactivator 1 (CRTC1), previously referred to as TORC1 (Transducer Of Regulated CREB activity 1),  is a protein that in humans is encoded by the CRTC1 gene. It is expressed in a limited number of tissues that include fetal brain and liver and adult heart, skeletal muscles, liver and salivary glands and various regions of the adult central nervous system.

# Clinical significance
Production of CRTC1 is blocked in Alzheimer's disease.
TORC1 might be the target protein in ketamin induced anti-depressent effect via NMDA-antagonisation.
The TORC1 inhibitor drugs dactolisib and everolimus, are being investigated to determine if they can boost the immunity of elderly patients.
CRYAA
Alpha-crystallin A chain is a protein that in humans is encoded by the CRYAA gene.
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC).

# Interactions
CRYAA has been shown to interact with CRYBB2, Hsp27, CRYGC and CRYAB.
CRYGC
Crystallin, gamma C, also known as CRYGC, is a protein which in humans is encoded by the CRYGC gene.

# Function
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.

# Interactions
CRYGC has been shown to interact with CRYBB2, CRYAA and CRYAB.
CRYGS
Gamma-crystallin S is a protein that in humans is encoded by the CRYGS gene.
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins.
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is monomeric and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant gamma-crystallin in adult eye lens tissue.
Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
CSMD1
CSMD1 CUB and Sushi multiple domains 1 is a protein that in humans is encoded by the CSMD1 gene.

# Structure
CSMD1 contains 14 N-terminal CUB domains that are separated from each other by a Sushi domains followed by an additional 15 tandem Sushi domain segment.

# Function
Based on analogy to other proteins that contain Sushi domains, it is believed that the gene product of CSMD1 functions as a Complement control protein.

# Clinical significance
It is a potential tumour suppressor, the deletion of which may result in head and neck carcinomas behaving more aggressively. CSMD1 protein expression was found to be reduced in patients with invasive breast cancer. Functional studies showed that CSMD1 reduction causes cells to transform to a cancer form by increasing their ability to divide, migrate and invade. In a three dimensional model of breast ducts, reduced CSMD1 expression failed breast duct formation.
CSPG4
Chondroitin sulfate proteoglycan 4, also known as melanoma-associated chondroitin sulfate proteoglycan (MCSP) or neuron-glial antigen 2 (NG2), is a chondroitin sulfate proteoglycan that in humans is encoded by the CSPG4 gene.
CSPG4 plays a role in stabilizing cell-substratum interactions during early events of melanoma cell spreading on endothelial basement membranes. It represents an integral membrane chondroitin sulfate proteoglycan expressed by human malignant melanoma cells.
CSPG4/NG2 is also a hallmark protein of oligodendrocyte progenitor cells (OPCs) and OPC dysfunction has been implicated as a candidate pathophysiological mechanism of familial schizophrenia. A research group investigating the role of genetics in schizophrenia, reported, two rare missense mutations in CSPG4 gene, segregating within families (CSPG4A131T and CSPG4V901G mutations). The researchers also demonstrate that the induced pluripotent stem cells (iPSCs)-derived OPCs from CSPG4A131T mutation carriers exhibited abnormal post-translational processing, subcellular localization of the mutant NG2 protein, aberrant cellular morphology, and a decreased cell viability and myelination potential. In vivo diffusion tensor imaging of the brain of CSPG4A131T mutation carriers demonstrated a reduced white matter integrity compared to the unaffected sibling and matched general population controls.
CSTF2
Cleavage stimulation factor 64 kDa subunit is a protein that in humans is encoded by the CSTF2 gene.
This gene encodes a nuclear protein with an RRM (RNA recognition motif) domain. The protein is a member of the cleavage stimulation factor (CSTF) complex that is involved in the 3' end cleavage and polyadenylation of pre-mRNAs. Specifically, this protein binds GU-rich elements within the 3'-untranslated region of mRNAs.

# Interactions
CSTF2 has been shown to interact with CSTF3, SUB1, SYMPK, BARD1 and BRCA1.
CTBP1
C-terminal-binding protein 1 also known as CtBP1 is a protein that in humans is encoded by the CTBP1 gene.

# Function
The CtBP1 protein was originally identified as a human protein that bound a PLDLS motif in the C-terminus of adenovirus E1A proteins. It and the related protein CTBP2 were later shown to function as transcriptional corepressors. That is, regulatory proteins that bind to sequence-specific DNA-binding proteins and help turn genes off. CtBPs do this by recruiting histone modifying enzymes that add repressive histone marks and remove activating marks. CtBP proteins can also self-associate and presumably bring together gene regulatory complexes.
CtBP1 is broadly expressed from embryo to adult, while CtBP2 has a somewhat more restricted pattern of expression. CtBPs have multiple biological roles and appear to be most important in regulating the epithelial to mesenchymal transition, as well as influencing metabolism. They do the latter by binding NADH in preference to NAD+, thereby sensing the NADH/NAD+ ratio. When bound it undergoes a conformational change that allows it to dimerize and associate with its partner proteins and silence specific genes.
During skeletal and T cell development, CtBP1 and CtBP2 associate with the PLDLSL domain of EF1, a cellular zinc finger-homeodomain protein, and thereby enhances EF1-induced transcriptional silencing. CtBP also binds the Kruppel-like factors family of zinc finger proteins KLF3, KLF8 and KLF12. In addition, CtBP complexes with CtIP, a 125 kDa protein that recognizes distinctly different protein motifs from CtBP. CtIP binds to the BRCT repeats within the breast cancer gene BRCA1 and enables CtBP to influence BRCA1 activity. Both proteins can also interact with a polycomb group protein complex which participates in regulation of gene expression during development. Alternative splicing of transcripts from this gene results in multiple transcript variants.

# Interactions
CTBP1 has been shown to interact with:
- ACTL6B,
- ARF,
- EVI1
- FOXP2,
- HDAC1,
- IKZF1,
- IKZF4,
- KLF3,
- KLF8,
- Mdm2,
- MLL,
- NRIP1,
- Pinin,
- RBBP8, and
- TGIF1.
- GATA1.
CTBP2
C-terminal-binding protein 2 also known as CtBP2 is a protein that in humans is encoded by the CTBP2 gene.

# Function
The CtBPs - CtBP1 and CtBP2 in mammals - are among the best characterized transcriptional corepressors. They typically turn their target genes off. They do this by binding to sequence-specific DNA-binding proteins that carry a short motif of the general form Proline-Isoleucine-Aspartate-Leucine-Serine (the PIDLS motif). They then recruit histone modifying enzymes, histone deacetylases, histone methylases and histone demethylases. These enzymes are thought to work together to remove activating and add repressive histone marks. For example, histone deacetylase 1 (HDAC1) and HDAC2 can remove the activating mark histone 3 acetyl lysine 9 (H3K9Ac), then the histone methylase G9a can add methyl groups, while the histone demethylase lysine specific demethylase 1 (LSD1) can remove the activating mark H3K4me.
The CtBPs bind to many different DNA-binding proteins and also bind to co-repressors that are themselves bound to DNA-binding proteins, such as Friend of GATA (Fog). CtBPs can also dimerize and multimerize to bridge larger transcriptional complexes. They appear to be primarily scaffold proteins that allow the assembly of gene repression complexes.
One interesting aspect of CtBPs is their ability to bind to NADH and to a lesser extent NAD+. It has been proposed that this will enable them to sense the metabolic status of the cell and to regulate genes in response to changes in the NADH/NAD+ ratio. Accordingly, CtBPs have been found to be important in fat biology, binding to key proteins such as PRDM16, NRIP, and FOG2.
The full functional roles of CtBP proteins in mammals have been difficult to evaluate because of partial redundancy between CtBP1 and CtBP2. Similarly, the early lethality of the CtBP2 knockout and of double knockout mice has precluded detailed analysis of the cellular effects of deleting these proteins. Important results have emerged from model organisms where there is only a single CtBP gene. In Drosophila CtBP is involved in development and in circadian rhythms. In the worm C. elegans CtBP is involved in life span. Both circadian rhythms and life span appear to be linked to metabolism supporting the role for CtBPs in metabolic sensing.
The mammalian CtBP2 gene produces alternative transcripts encoding two distinct proteins. In addition to the transcriptional repressor (corepressor) discussed above, there is a longer isoform that is a major component of specialized synapses known as synaptic ribbons. Both proteins contain a NAD+ binding domain similar to NAD+-dependent 2-hydroxyacid dehydrogenases. A portion of the 3'-untranslated region was used to map this gene to chromosome 21q21.3; however, it was noted that similar loci elsewhere in the genome are likely. Blast analysis shows that this gene is present on chromosome 10.

# Interactions
CTBP2 has been shown to interact with:
- FHL3,
- KLF3,
- KLF8,
- Mdm2,
- NRIP1,
- SOX6,  and
- ZFPM2.
CTDP1
RNA polymerase II subunit A C-terminal domain phosphatase is an enzyme that in humans is encoded by the CTDP1 gene.
This gene encodes a protein which interacts with the carboxy-terminus of transcription initiation factor TFIIF, a transcription factor which regulates elongation as well as initiation by RNA polymerase II. The protein may also represent a component of an RNA polymerase II holoenzyme complex. Alternative splicing of this gene results in two transcript variants encoding 2 different isoforms.

# Interactions
CTDP1 has been shown to interact with WD repeat-containing protein 77, GTF2F1 and POLR2A.
CUTL1
Cux1 (CUTL1, CDP, CDP/Cux) is a homeodomain protein that in humans is encoded by the CUX1 gene.

# Function
The protein encoded by this gene is a member of the homeodomain family of DNA binding proteins. It regulates gene expression, morphogenesis, and differentiation and it also plays a role in cell cycle progression, particularly at S-phase. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined, and the p200 isoform of Cux1 is processed proteolytically to  smaller active isoforms, such as p110. Cux1 DNA binding is stimulated by activation of the PAR2/F2RL1 cell-surface G-protein-coupled receptor in fibroblasts and breast-cancer epithelial cells to regulate Matrix metalloproteinase 10, Interleukin1-alpha, and Cyclo-oxygenase 2 (COX2) genes.

# Role in tumor growth
Genetic data from over 7,600 cancer patients shows that over 1% has the deactivated CUX1 which links to progression of tumor growth.  Researchers from the Wellcome Trust Sanger Institute reported that the mutation of CUX1 reduces the inhibitory effects of a biological inhibitor, PIK3IP1 (phosphoinositide-3-kinase interacting protein 1), resulted in higher activity of the growth promoting enzyme, phosphoinositide 3-kinase (PI3K) which leads to tumor progression.  Although CUX1 is mutated at a lower rate compared to other known gene mutations that cause cancer, this deactivated gene is found across many cancer types in this study to be the underlying cause of the disease.

# CASP
Tne CUX1 gene Alternatively Spliced Product was first reported in 1997. The CUX1 gene has up to 33 exons. CASP mRNA includes exons 1 through 14 and 25 through 33. The human CASP protein is predicted to contain 678 amino acids, of which 400 are shared with CUTL1. CASP protein is approximately 80 kD. It lacks the DNA binding region of CUTL1, but instead contains a trans-membrane domain that allows it to insert into lipid bilayers. It has been localized to the Golgi apparatus.
CASP has been reported to be part of a complex with Golgin 84 that tethers COPI vesicles and is important for retrograde transport in the Golgi and between the Golgi and endoplasmic reticulum. The targeting of vesicles involves tethers and SNAREs.

# Interactions
Cux1 (CUTL1, CDP, CDP/Cux) has been shown to interact with:
- CREB binding protein,
- Retinoblastoma protein, and
- SATB1
These physical interactions are reported in BioPlex 2.0
- MAGEA10
- EXT2
- RAB30
- HLA-DQA1
- STX6
- WDR83
- SLC39A4
- LAMP1
- POTEB
- SLC39A12

# Notes
-  This CASP is not the same as the scaffolding protein called CASP for Cytohesin/ARNO ... Scaffolding Protein
CXCL1
The chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, GRO, KC, neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MGSA-).  In humans, this protein is encoded by the Cxcl1.

# Function
CXCL1 is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis.
CXCL1 is expressed by macrophages, neutrophils and epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, arteriogenesis, inflammation, wound healing, and tumorigenesis.
This chemokine elicits its effects by signaling through the chemokine receptor CXCR2.  The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines. An initial study in mice showed evidence that CXCL1 decreased the severity of multiple sclerosis and may offer a neuro-protective function.
CXCL5
C-X-C motif chemokine 5 (CXCL5 or ENA78) is a protein that in humans is encoded by the CXCL5 gene.

# Function
The protein encoded by this gene, CXCL5 is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78).  It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II interferon IFN-. This chemokine stimulates the chemotaxis of neutrophils possessing angiogenic properties.  It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling. CXCL5 has been also described to regulate neutrophil homeostasis.

# Clinical significance
CXCL5 plays a role in reducing sensitivity to sunburn pain in some subjects, and is a "potential target which can be utilized to understand more about pain in other inflammatory conditions like arthritis and cystitis.". CXCL5 is well known to have chemotactic and activating functions on neutrophil, mainly during acute inflammatory responses. However CXCL5 expression is also higher in atherosclerosis (a chronic inflammatory condition) but is not associated with neutrophil infiltration. Instead CXCL5 has a protective role in atherosclerosis by directly controlling macrophage foam cell formation.
CXCL9
Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belonging to the CXC chemokine family that is also known as Monokine induced by gamma interferon (MIG).  CXCL9 is a T-cell chemoattractant, which is induced by IFN-. It is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.
Neutrophil collagenase/matrix metalloproteinase 8 (MMP-8) degrades CXCL9 and cleaves CXCL10 at two positions.
Gelatinase B/matrix metalloproteinase 9 (MMP-9) degrades CXCL10 and cleaves CXCL9 at three different sites in its extended carboxy-terminal region.

# Biomarkers
CXCL9, -10, -11 have proven to be valid biomarkers for the development of heart failure and left ventricular dysfunction, suggesting an underlining pathophysiological relation between levels of these chemokines and the development of adverse cardiac remodeling.
This chemokine has also been associated as a biomarker for diagnosing Q fever infections.

# Interactions
CXCL9 has been shown to interact with CXCR3.