Persius/hicric huggingface dataset:
CKMT1A
Creatine kinase U-type, mitochondrial, also called ubiquitous mitochondrial creatine kinase (uMtCK), is in humans encoded by CKMT1A gene. CKMT1A catalyzes the reversible transfer of the -phosphate group of ATP to the guanidino group of Cr to yield ADP and PCr. The impairment of CKMT1A has been reported in ischaemia, cardiomyopathy, and neurodegenerative disorders. Overexpression of CKMT1A has been reported related with several tumors.

# Structure

## Gene
The CKMT1A gene lies on the chromosome location of 15q15.3 and consists of 11 exons.

## Protein
CKMT1A consists of 417 amino acids and weighs 47037Da. CKMT1A is rich in amino acids with hydroxyl-containing and basic side chains.

# Function
There are four distinct types of CK subunits in the tissue of mammals, which are expressed species specifically, developmental stage specifically, and tissue specifically. Ubiquitously expressed, CKMT1A is located in the mitochondrial intermembrane space and form both homodimeric and homooctameric molecules that are readily interconvertible. Like all the other CK isoenzymes, CKMT1A catalyzes the reversible transfer of the -phosphate group of ATP to the guanidino group of Cr to yield ADP and PCr. According to the transport (shuttle) hypothesis for the CK system, after synthesis within the mitochondrial matrix, the -phosphate group of ATP is transferred by CKMT1A in the mitochondrial intermembrane space to Cr to yield ADP plus PCr.

# Clinical significance
As an enzyme central to cell energetics, CKMT1A is often impaired in pathological situations. CKMT1A is known as a primary target of oxidative and radical-induced molecular damage; and the impairment of CKMT1A has been reported in ischaemia, cardiomyopathy, and neurodegenerative disorders due to the failure in maintaining metabolic homeostasis. Overexpression of uMtCK has been reported for several tumors with poor prognosis and this may be the adaption of cancer cells to maintain the high growth rate.

# Interactions
- Leucine-rich repeat kinase 
- ASB9
CKMT1B
Creatine kinase, mitochondrial 1B also known as CKMT1B is one of two genes which encode the ubiquitous mitochondrial creatine kinase (ubiquitous mtCK or CKMT1).

# Function
Mitochondrial creatine (MtCK) kinase is responsible for the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. It belongs to the creatine kinase isoenzyme family. It exists as two isoenzymes, sarcomeric MtCK (CKMT2) and ubiquitous MtCK, encoded by separate genes. Mitochondrial creatine kinase occurs in two different oligomeric forms: dimers and octamers, in contrast to the exclusively dimeric cytosolic creatine kinase isoenzymes. Ubiquitous mitochondrial creatine kinase has 80% homology with the coding exons of sarcomeric mitochondrial creatine kinase. Two genes located near each other on chromosome 15 (CKMT1A and CKMT1B (this gene)) have been identified which encode identical mitochondrial creatine kinase proteins.

# Clinical significance
Many malignant cancers with poor prognosis have shown overexpression of ubiquitous mitochondrial creatine kinase; this may be related to high energy turnover and failure to eliminate cancer cells via apoptosis.
CLDN14
Claudin-14 is a protein that in humans is encoded by the CLDN14 gene. It belongs to a related family of proteins called claudins.
The protein encoded by CLDN14 is an integral membrane protein and a component of tight junctions, one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets. Tight junctions form continuous seals around cells and serve as a physical barrier to prevent solutes and water from passing freely through the paracellular space.
These junctions are composed of sets of continuous networking protein strands in the outer surface of the cell membrane, with complementary grooves in the inwardly facing extracytoplasmic leaflet.  The CLDN14 protein also binds to particular part of a protein called Yes-associated protein, known as its WW domain.
Defects in CLDN14 are the cause of an autosomal recessive form of nonsyndromic sensorineural deafness. Two transcript variants encoding the same protein have been found for this gene.
There are also suggestions that CLDN14 plays a role in tumour angiogenesis (blood vessel formation), as deletion of a single copy of this gene leads to tight junction defects and leaky blood vessels in a mouse model.
CLDN16
Claudin-16 is a protein that in humans is encoded by the CLDN16 gene. It belongs to the group of claudins.
Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. These junctions are composed of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet, with complementary grooves in the inwardly facing extracytoplasmic leaflet. The protein encoded by this gene, a member of the claudin family, is an integral membrane protein and a component of tight junction strands. It is found primarily in the kidneys, specifically in the thick ascending limb of Henle, where it acts as either an intercellular pore or ion concentration sensor to regulate the paracellular resorption of magnesium ions. Defects in this gene are a cause of primary hypomagnesemia, which is characterized by massive renal magnesium wasting with hypomagnesemia and hypercalciuria, resulting in nephrocalcinosis and renal failure.

# Model organisms
Model organisms have been used in the study of CLDN16 function. A conditional knockout mouse line, called Cldn16tm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty five tests were carried out on homozygous mutant animals and one significant abnormality was observed: the mice displayed urolithiasis.
CLDN18
Claudin-18 is a protein that in humans is encoded by the CLDN18 gene. It belongs to the group of claudins.
CLDN18 belongs to the large claudin family of proteins, which form tight junction strands in epithelial cells . 

# Clinical significance
Isoform 2 (Claudin 18.2) is abundant in gastric tumors.
Experimental antibody IMAB362 targets Claudin 18.2 to help treat gastric cancers.
CLEC2D
C-type lectin domain family 2 member D is a protein that in humans is encoded by the CLEC2D gene.
This gene encodes a member of the natural killer cell receptor C-type lectin family. The encoded protein inhibits osteoclast formation and contains a transmembrane domain near the N-terminus as well as the C-type lectin-like extracellular domain. Several alternatively spliced transcript variants have been identified, but the full-length nature of every transcript has not been defined.  CLEC2D encodes the gene for the Lectin Like Transcript-1 (LLT1) protein which is a functional ligand for the human NKR-P1A receptor, encoded by the KLRB1 gene.
In mice, there are many orthologs of the CLEC2D gene, and the presumed homolog is Clr-b/Ocil (Clec2d). Clr-b has been implicated in missing-self recognition by natural killer cells through engagement of the NKR-P1B receptor.
CLINT1
Clathrin interactor 1 (CLINT1), also known as EPSIN4, is a protein which in humans is encoded by the CLINT1 gene.

# Function
The CLINT1 protein binds to the terminal domain of the clathrin heavy chain and stimulates clathrin cage vesicle assembly. Clathrin coated vesicles enable neurotransmitter receptors and other proteins to be endocytosed or taken up across neuronal membranes and across the membranes of other types of cells. This enables a turnover of neuroreceptors or other proteins to be maintained and thus the numbers of receptors can be fine tuned.

# Clinical significance
The CLINT1 gene has been shown to be involved in the genetic aetiology of schizophrenia in four studies  It is known that the  antipsychotic drugs chlorpromazine and clozapine stabilise clathrin coated vesicles and this may be one reason why antipsychotic drugs are effective in treating delusions, auditory hallucinations and many of the other symptoms of schizophrenia.

# Interactions
CLINT1 has been shown to interact with GGA2.
CLSTN1
Calsyntenin-1 is a protein that in humans is encoded by the CLSTN1 gene.

# Clinical relevance
Mutations in this gene have been shown associated to pathogenic mechanisms of Alzheimer's disease.

# Interactions
CLSTN1 has been shown to interact with APBA2 and Amyloid precursor protein.
CLUAP1
Clusterin associated protein 1, also known as CLUAP1, is a human gene.

# Model organisms
Model organisms have been used in the study of CLUAP1 function. A conditional knockout mouse line, called Cluap1tm1a(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 six 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; both sexes had decreased IgG1 levels while males also displayed abnormal spine curvature resulting in kyphosis.
CMKLR1
Chemokine like receptor 1  also known as ChemR23 (Chemerin Receptor 23) is a protein that in humans is encoded by the CMKLR1 gene. Chemokine receptor-like 1 is a G protein-coupled receptor for the chemoattractant adipokine chemerin and the omega-3 fatty acid eicosapentaenoic acid-derived specialized pro-resolving molecule, resolvin E1 (see Specialized proresolving mediators#EPA-derived resolvins (i.e. RvE)). The murine receptor that shares almost 80% homology with the human receptor, is called Dez.

# Tissue distribution
CMKLR1 shows wide RNA expression profile but is notably high in plasmacytoid dendritic cells, macrophages, cardiomyocytes, adipocytes and endothelial cells.

# Function
Activating CMKLR1 by an agonist mobilizes intracellular calcium and causes the activation of several other signaling cascades like the ERK1 and NF-B. Initial studies of CMKLR1 suggested that it might have a role in the inflammatory pathways. Its cognate ligand, chemerin was found in joint aspirate from rheumatoid arthritis and absent in aspirate from degenerative arthritis. CMKLR1 expression by plasmacytoid dendritic cells and macrophages also helped foster this idea. In vitro chemotaxis assays showed it to be utilized in attracting these cells. As an adipokine receptor it has a role in adipogenesis and adipocyte maturation. It seems also to have a role in peripheral insulin resistance.
Also studies using the mouse zymosan model and chemerin peptides showed that these peptides suppressed and helped resolve the peritonitis in mice. The same model showed that this particular molecule enhances macrophage efferocytosis (phagocyting apoptotic cells).

# Receptor antagonist CCX832
CCX832 is an orally active molecule used as a tool compound in experimental pharmacology. It antagonises the effect of CMKLR1. It is listed on the Guide to Pharmacology database as the only example of a CMKLR1 antagonist. Its chemical structure is undisclosed.
The substance was originally developed for use as a pharmaceutical drug against inflammatory diseases by ChemoCentryx, a pharmaceutical firm based in California, in alliance with GlaxoSmithKline (GSK). Development was terminated after a Phase I clinical trial in 2012.
CNKSR2
Connector enhancer of kinase suppressor of ras 2, also known as CNK homolog protein 2 (CNK2) or maguin (membrane-associated guanylate kinase-interacting protein), is an enzyme that in humans is encoded by the CNKSR2 gene.

# Function
CNKSR2 is a multidomain protein that functions as a scaffold protein to mediate the mitogen-activated protein kinase pathways downstream from Ras. This gene product is induced by vitamin D and inhibits apoptosis in certain cancer cells. It may also play a role in ternary complex assembly of synaptic proteins at the postsynaptic membrane and coupling of signal transduction to membrane/cytoskeletal remodeling.

# Mechanism of action
It is the mammalian homolog of the Drosophilia gene Cnk, which is known to bind Raf, and is implicated in ras signalling. It has been show that CNKSR2 is also a Raf binding protein, and is assumed to function in bringing together the Ras signalling complex at the post synaptic density.
It is known to have two isoforms, one of which binds PSD95 and S-SCAM (synaptic scaffolding molecule) through its PDZ domain, and another which does not. Both of the isoforms are, however, known to be synaptically localized, and it is understood that this is mediated by the Pleckstrin homology domain. It's synaptic localization is not known to be affected by NMDA receptor activation. Overexpression of Maguin's C-terminal PDZ domain is known to repress synaptic localization of PSD95. In cultures, MAGUIN colocalizes with PSD95 and synaptophysin at puncta in neurites, and these puncta are first visible at 6DIV.
Proteomic work done on binding partners of Ksr2 suggests that the CNKSR2/KSR2 complex may play a role in mediating crosstalk between the MAPK, Pi3K and insulin pathways. It was found to form a complex with MEK1 (Erk2, p38), MEK2, cdk4, PI3k, the phosphatases PP2A and PP^, and also various translational, ribosomal, transport and structural proteins. It remains to be established how many of these are affected by CNKSR2, and whether this remains true for Ksr2 in the nervous system.
Densin-180 is another important synaptic protein found to interact with CNKSR2. It is known to bind at its C-terminal PDZ domain. In transfected cells, no association could be found between PSD95 and Densin-180 without the presence of CNKSR2. This brings it into a complex with CamKII and -catenin, and further to the binding partners of CNKSR2 suggest that CNKSR2 may have a role in dendritic branching.
COL3A1
Collagen, type III, alpha 1 (Ehlers-Danlos syndrome type IV, autosomal dominant), also known as COL3A1, is a human gene.
This gene encodes a fibrillar collagen that is found in extensible connective tissues such as skin, lung, and the vascular system, frequently in association with type I collagen. Mutations in this gene are associated with Ehlers-Danlos syndrome type IV, and with aortic and arterial aneurysms. Although alternate transcripts have been detected for this gene, they are the result of mutations; these mutations alter splicing, often leading to the exclusion of multiple exons.
Type-III collagen is a fibrous scleroprotein in bone, cartilage, tendon, bone marrow stroma  and other connective tissue; yields gelatin on boiling.
Scleroprotein is a simple protein found in horny and cartilaginous tissues and in the lens of the eye.
COL4A1
Collagen, type IV, alpha 1, also known as COL4A1, is a human gene.
This gene encodes the major type IV alpha collagen chain of basement membranes. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter.
Mutations in COL4A1 exons 24 and 25 are associated with HANAC (autosomal dominant hereditary angiopathy with nephropathy, aneurysms, and muscle cramps).
CORO1B
Coronin, actin binding protein, 1B also known as CORO1B is a protein which in humans is encoded by the CORO1B gene. Members of the coronin family, such as CORO1B, are WD repeat-containing actin-binding proteins that regulate cell motility.

# Function
A mammalian coronin enriches at the leading edge of migrating cells. Studies related to this protein are as follows:
- Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia.
- F-actin binding is essential for coronin 1B function in vivo.
- Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge.
- Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility.
- In vivo and in vitro characterization of novel neuronal plasticity factors identified following spinal cord injury.
- Isolation, cloning, and characterization of a new mammalian coronin family member, coroninse, which is regulated within the protein kinase C signaling pathway.
COX4I1
Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (COX4I1) is an enzyme that in humans is encoded by the COX4I1 gene. COX4I1 is a nuclear-encoded isoform of cytochrome c oxidase (COX) subunit 4. Cytochrome c oxidase (complex IV) is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane, acting as the terminal enzyme of the mitochondrial respiratory chain. Antibodies against COX4 can be used to identify the inner membrane of mitochondria in immunfluorescence studies. Mutations in COX4I1 have been associated with COX deficiency and Fanconi anemia.

# Structure
COX4I1 is located on the q arm of chromosome 16 in position 24.1 and has 6 exons. The COX4I1 gene produces a 9.3 kDa protein composed of 83 amino acids. COX4I1 is expressed ubiquitously. The protein encoded by COX4I1 belongs to the cytochrome c oxidase IV family. COX4I1 has a transit peptide domain and acetyl and phosphoprotein amino acid modifications. It is located at the 3' of the NOC4 (neighbor of COX4) gene in a head-to-head orientation, and shares a promoter with it.

# Function
COX4I1 encodes a protein that is located in the inner mitochondrial membrane and is an isoform of the nuclear-encoded subunit IV of cytochrome c oxidase (complex IV), the terminal oxidase in mitochondrial electron transport. Complex IV is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. The expression of COX4I1, along with COX4I2, may be regulated by oxygen levels, with reduced levels of oxygen leading to increased COX4I2 expression and COX4I1 degradation. This suggests a role for COX4I1 in the optimization of the electron transfer chain under different conditions.

# Clinical Significance
Although relatively little is known about the function of COX4I1, mutations in this gene have been associated with mitochondrial complex IV diseases with severe phenotypes. Among these, COX deficiency and Fanconi anemia have been suspected and linked to mutations in the COX4I1 gene. Clinical features of pathogenic variants of COX4I1 can include short stature, poor weight gain, mild dysmorphic features, mental retardation, spastic paraplegia, severe epilepsy, a narrow and arched palate, malar hypoplasia, little subcutaneous fat, and arachnodactyly. The homozygous mutation K101N and a de novo 16q24.1 interstitial duplication have been found to cause defective COX4I1.

# Interactions
COX4I1 has 153 protein-protein interactions with 142 of them being co-complex interactions. COX4I1 has been found to interact with SDCBP, MT-CO1, IKBKE, TMBIM4, and MCL1.
COX6A1
Cytochrome c oxidase subunit 6A1, mitochondrial is an protein that in humans is encoded by the COX6A1 gene. Cytochrome c oxidase 6A1 is a subunit of the cytochrome c oxidase complex, also known as Complex IV, the last enzyme in the mitochondrial electron transport chain. A mutation of the COX6A1 gene is associated with a recessive axonal or mixed form of Charcot-Marie-Tooth disease.

# Structure
The COX6A1 gene, located on the q arm of chromosome 12 in position 24.2, contains 3 exons and is 2,653 base pairs in length. The COX6A1 protein weighs 12 kDa and is composed of 109 amino acids. The protein is a subunit of Complex IV, a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. This nuclear gene encodes polypeptide 1 (liver isoform) of subunit VIa, and polypeptide 1 is found in all non-muscle tissues. Polypeptide 2 (heart/muscle isoform) of subunit VIa is encoded by a different gene, COX6A2, and is present only in striated muscles. These two polypeptides share 66% amino acid sequence identity.

# Function
Cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane to drive ATP synthesis via protonmotive force.  The mitochondrially-encoded subunits perform the electron transfer of proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex.
Summary reaction:

# Clinical significance
A mutation leading to a 5 base pair deletion in the COX6A1 gene is associated with Charcot-Marie-Tooth disease (CMT). CMT is the most common inherited neuropathy and can result from mutations in over 30 different loci. Expression of COX6A1 is significantly reduced in affected individuals.
The Trans-activator of transcription protein (Tat) of human immunodeficiency virus (HIV) inhibits cytochrome c oxidase (COX) activity in permeabilized mitochondria isolated from both mouse and human liver, heart, and brain samples. Rapid loss of membrane potential (m) occurs with submicromolar doses of Tat, and cytochrome c is released from the mitochondria.
COX6A2
Cytochrome c oxidase subunit VIa polypeptide 2 is a protein that in humans is encoded by the COX6A2 gene. Cytochrome c oxidase 6A2 is a subunit of the cytochrome c oxidase complex, also known as Complex IV, the last enzyme in the mitochondrial electron transport chain.

# Structure
The COX6A2 gene, located on the p arm of chromosome 16 in position 11.12, contains 3 exons and is 698 base pairs in length. The COX6A1 protein weighs 11 kDa and is composed of 97 amino acids. The protein is a subunit of Complex IV, a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. This nuclear gene encodes polypeptide 2 (heart/muscle isoform) of subunit VIa, and polypeptide 2 is present only in striated muscles. Polypeptide 1 (liver isoform) of subunit VIa is encoded by a different gene, COX6A1, and is found in all non-muscle tissues. These two polypeptides share 66% amino acid sequence identity.

# Function
Cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane to drive ATP synthesis via protonmotive force.  The mitochondrially-encoded subunits perform the electron transfer of proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex.
Summary reaction:

# Clinical significance
The Trans-activator of transcription protein (Tat) of human immunodeficiency virus (HIV) inhibits cytochrome c oxidase (COX) activity in permeabilized mitochondria isolated from both mouse and human liver, heart, and brain samples. Rapid loss of membrane potential (m) occurs with submicromolar doses of Tat, and cytochrome c is released from the mitochondria.