Persius/hicric huggingface dataset:
3T3-L1
3T3-L1 is a cell line derived from 3T3 cells that is used in bilogical research on adipose tissue. 3T3-L1 cells have a fibroblast-like morphology, but, under appropriate conditions, the cells differentiate into an adipocyte-like phenotype.
3T3-L1 cells of the adipocyte morphology increase the synthesis and accumulation of triglycerides and acquire the signet ring appearance of adipose cells. These cells are also sensitive to lipogenic and lipolytic hormones and drugs, including epinephrine, isoproterenol, and insulin.

# Sources
-  Green H, Kehinde O (1975). "An established preadipose cell line and its differentiation in culture. II. Factors affecting the adipose conversion". Cell. 5 (1): 1927. PMID 165899..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"\"""\"""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{display:none;font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
ABCA12
ATP-binding cassette sub-family A member 12 also known as ATP-binding cassette transporter 12 is a protein that in humans is encoded by the ABCA12 gene.
ABCA12 belongs to a group of genes called the ATP-binding cassette family, which makes proteins that transport molecules across cell membranes. The ABCA12 gene is active in some types of skin cells and in several other tissues, such as testis, placenta, lung, stomach, and fetal brain and liver. This protein appears to be essential for normal development of the skin, which provides a barrier between the body and its surrounding environment.  It transports epidermoside, a glucosylceramide, out of the keratinocytes of the stratum corneum of the epidermis.
The ABCA12 gene is located on the long (q) arm of chromosome 2 between positions 34 and 35, from base pair 215,621,772 to base pair 215,828,656.

# Related conditions
Several mutations in the ABCA12 gene are known to cause harlequin-type ichthyosis. Most of these mutations are predicted to lead to an absence of ABCA12 protein or the production of an extremely small version of the protein that cannot transport lipids properly. A loss of functional ABCA12 protein causes numerous problems with the development of the epidermis before and after birth. Abnormalities in lipid transport prevent the skin from forming an effective barrier and result in the hard, thick scales characteristic of harlequin ichthyosis.
Mutations in the ABCA12 gene also cause another severe skin disorder, lamellar ichthyosis type 2. People with this disorder have red, scaly, plate-like skin covering most of their bodies. The ABCA12 mutations that cause this disorder substitute one amino acid (a building block of proteins) for another amino acid in the ABCA12 protein. These mutations almost always occur in an important functional region of the protein (the region that binds to ATP, a molecule that supplies energy for chemical reactions). Changes in the structure of the ABCA12 protein likely disrupt its ability to transport lipids, which affects the development of skin before and after birth.
ABCB11
ATP-binding cassette, sub-family B member 11 also known as ABCB11 is a protein which in humans is encoded by the ABCB11 gene.

# Function
The product of the ABCB11 gene is an ABC transporter named BSEP (Bile Salt Export Pump), or sPgp (sister of P-glycoprotein). This membrane-associated protein is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White).
This protein is a member of the MDR/TAP subfamily. Some members of the MDR/TAP subfamily are involved in multidrug resistance. This particular protein is responsible for the transport of taurocholate and other cholate conjugates from hepatocytes (liver cells) to the bile. In humans, the activity of this transporter is the major determinant of bile formation and bile flow.

# Clinical significance
ABCB11 is a gene associated with progressive familial intrahepatic cholestasis type 2 (PFIC2). PFIC2 caused by mutations in the ABCB11 gene increases the risk of hepatocellular carcinoma in early life.
ABHD18
ABHD18 is a protein that in Homo sapiens is encoded by the ABHD18 gene.

# Gene
ABHD18 is found on the positive strand of the human genome at 4q28.2. It is 74.4 kbp. The gene contains 17 exons. The longest mRNA transcript is composed of 13 exons and is 2200 base pairs.

# Homology

## Orthologs
Many orthologs to human ABHD18 have been discovered, with the most distant ortholog with high (over 90%) coverage is found in rice Oryza sativa. The protein is not found in fungi. Bacteria of the order Myxobacteria and genus Chitinimonas contain orthologous regions to the C4orf29 protein. The few bacterial homologs indicate a horizontal gene transfer event. The domain of unknown function, DUF2048, is conserved throughout orthologs.

# Protein
ABHD18 codes a 414 amino acid sequence of 46.9 kDa in humans. The predicted isoelectric point is 9.37. The domain of unknown function, DUF2048, is found from amino acid residues 25 to 414 in the precursor C4orf29 protein. This domain is part of the alpha/beta hydrolase superfamily, which comprises enzymes that catalyze fat metabolism. Predicted post-translational modifications include glycosylation at residues Ser287 and Ser319  and sumoylation at the motifs Phe240 to Gly243, Ala377 to Asp340, and Phe408 to Gly411.

# Expression
The protein product of ABHD18 in humans is predicted to be a secreted product. It is ubiquitously expressed at low to moderate levels. In humans, the protein is found at high levels the digestive tract and parathyroid gland. The homologous mouse protein 3110057O12Rik is expressed at high levels in the granule layer of the cerebellum.

# Clinical significance
ABHD18 contains highly variable numbers of Alu repeats. A low number of Alu repeats in the human ABHD18 protein is associated with increase prevalence of hepatocellular carcinoma (HCC) in Asian populations. This information is used as a genetic marker to determine genetic risk of HCC. 
Swine muscle transcriptome analysis indicates high expression of ABHD18 in swine with extreme low levels of fatty acid composition.
ABLIM3
Actin-binding LIM protein 3 is a protein that in humans is encoded by the ABLIM3 gene.

# Function
The LIM domain is a double zinc finger structure that promotes protein-protein interactions. LIM domain proteins, such as ABLIM3, play roles in embryonic development, cell lineage determination, and cancer. An important paralog of this gene is LIMS1.

# Clinical relevance
Diseases associated with ABLIM3 include hepatoblastoma, and among its related super-pathways are axon guidance and DCC mediated attractive signaling.
ACAD10
Acyl-CoA dehydrogenase family, member 10 is a protein that in humans is encoded by the ACAD10 gene.

# Structure
This gene encodes a member of the acyl-CoA dehydrogenase family of enzymes (ACADs), which participate in the beta-oxidation of fatty acids in mitochondria. The encoded enzyme contains a hydrolase domain at the N-terminal portion, a serine/threonine protein kinase catalytic domain in the central region, and a conserved ACAD domain at the C-terminus. 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.

# Clinical significance
In Pima people, ACAD10 has been identified as a gene associated with type 2 diabetes, insulin resistance, and impaired lipid metabolism. Specifically, two single nucleotide polymorphisms, rs601663 and rs659964, have been significantly correlated with these symptoms in a large population of both the Pima people and American Indians.

# Interactions
Using affinity capture mass spectrometry, an interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. Using this method, ACAD10 has been shown to interact with P2RY8, NDUFA10, NTRK3, SLC2A12, LPAR4, PTH1R, COLEC10, APP, MAS1, CD79A, BSG, and Ubiquitin C.
ACADSB
ACADSB is a human gene that encodes short/branched chain specific acyl-CoA dehydrogenase (SBCAD), an enzyme in the acyl CoA dehydrogenase family.
It can cause short/branched-chain acyl-CoA dehydrogenase deficiency.

# Structure
The human ACADSB gene is located on chromosome 10; its exact localization has been identified as 10q25-q26. The open reading frame (ORF) encodes a precursor protein that contains 431 amino acids; post-translational processing results in a mature protein with 399 amino acids. The cDNA is significantly similar to the cDNA of other members of the acyl-CoA dehydrogenase family; its structure is closest to that of short chain acyl-CoA dehydrogenase. The structure of the catalytic pocket has also been studied; position 104 at the bottom of the substrate-binding pocket has been identified as important in determining the length of the primary carbon chain that can be accommodated. Altering residues at positions 105 and 177 have been demonstrated to affect the rate of the dehydrogenation reactions.

# Function
Short/branched chain acyl-CoA dehydrogenase(ACADSB) is a member of the acyl-CoA dehydrogenase family of enzymes that catalyze the dehydrogenation of acyl-CoA derivatives in the metabolism of fatty acids or branch chained amino acids. Substrate specificity is the primary characteristic used to define members of this gene family. The ACADSB gene product has the greatest activity towards the short branched chain acyl-CoA derivative, (S)-2-methylbutyryl-CoA, but also reacts significantly with other 2-methyl branched chain substrates and with short straight chain acyl-CoAs. The encoded protein is also involved in L-leucine catabolism.

# Clinical significance
Mutations in the ACADSB gene have been associated with 2-Methylbutyryl-CoA dehydrogenase deficiency (SBCADD, also known as MBD) deficiency, an autosomal recessive metabolic disorder of impaired isoleucine degradation. Many mutations across the genes 10 exons have been identified, with the mutations causing exon skipping and other transcriptional and translational errors. The disorder may be detected by MS/MS-based routine newborn screening due to the heightened presence of 2-methylbutyrylcarnitine in tissue samples. The disorder may also be identified using urinary organic acid analysis, by detecting the presence of 2-methylbutyryl glycinuria. While many individuals with a mutation in this gene may be asymptomatic, some patients have been reported to have symptoms in early infancy. Infants may experience apneic episodes, generalized muscle atrophy, hypotonia, lethargy, seizures, and delayed motor development. Patients may also experience metabolic symptoms such as hypothermia and hypoglycemia. Finally, genetic polymorphisms of the ACADSB gene may also be involved in the development of hypertension in the Japanese population.
ACADVL
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial (VLCAD) is an enzyme that in humans is encoded by the ACADVL  gene.
Mutations in the ACADVL are associated with very long-chain acyl-coenzyme A dehydrogenase deficiency. The protein encoded by this gene is targeted to the inner mitochondrial membrane, where it catalyzes the first step of the mitochondrial fatty acid beta-oxidation pathway. This acyl-Coenzyme A dehydrogenase is specific to long-chain and very-long-chain fatty acids. A deficiency in this gene product reduces myocardial fatty acid beta-oxidation and is associated with cardiomyopathy. Alternative splicing results in multiple transcript variants encoding different isoforms.

# Structure
The ACADVL gene contains 20 exons, and is about 5.4 kb long. VLCAD has interesting gene structure in humans, in that is located in a head-to-head structure with the DLG4 gene on Chromosome 17, and that the transcribed regions of these genes overlap. It has been shown that treatment with DEHP results in upregulation by the minimal promoter. While DLG4 and VLCAD share common regulatory elements, they each have separate and distinct tissue-specific elements that confer their function. In mice, these two genes are in a head-to-head orientation, but they do not overlap.

# Function
The VLCAD enzyme catalyzes most of fatty acid beta-oxidation by forming a C2-C3 trans-double bond in the fatty acid. VLCAD is specific to very long-chain fatty acids, typically C16-acylCoA and longer. In mice that have VLCAD deficiency, there is little to no protein hyperacetylation in the liver; this implies that the VLCAD protein is also necessary for protein acetylation in this biological system.

# Clinical significance
ACADVL is linked with very long-chain acyl-coenzyme A dehydrogenase deficiency (VLCADD), which has many symptoms, and typically presents as one of three phenotypes. The first is severe, with an early childhood onset and high mortality rate; the most common symptom is this form is cardiomyopathy. The second is a late onset childhood form, with milder symptoms that present most commonly as hypoketotic hypoglycemia. The final form presents in adulthood, and presents as isolated skeletal muscle involvement, rhabdomyolysis, and myoglobinuria, which is triggered by exercise or fasting. The disease is typically diagnosed by first performing tandem mass spectrometry on a blood sample of the patient during a period of stress, and then performing molecular genetic testing for the presence of the ACADVL gene. The deficiency is treated systematically, but certain conditions such as fasting, myocardial irritation, dehydration, and high fat diets are avoided in attempt to prevent secondary complications.

# Interactions
ACADVL has been shown to have 75 binary protein-protein interactions including 73 co-complex interactions. ACADVL appears to interact with RPSA and GPHN.
ACOT13
Acyl-CoA thioesterase 13 is a protein that in humans is encoded by the ACOT13 gene. This gene encodes a member of the thioesterase superfamily. In humans, the protein co-localizes with microtubules and is essential for sustained cell proliferation.

# Structure
The orthologous mouse protein forms a homotetramer and is associated with mitochondria. The mouse protein functions as a medium- and long-chain acyl-CoA thioesterase. Multiple transcript variants encoding different isoforms have been found for this gene.

# Function
The protein encoded by the ACOT13 gene is part of a family of Acyl-CoA thioesterases, which catalyze the hydrolysis of various Coenzyme A esters of various molecules to the free acid plus CoA. These enzymes have also been referred to in the literature as acyl-CoA hydrolases, acyl-CoA thioester hydrolases, and palmitoyl-CoA hydrolases. The reaction carried out by these enzymes is as follows:
CoA ester + H2O  free acid + coenzyme A
These enzymes use the same substrates as long-chain acyl-CoA synthetases, but have a unique purpose in that they generate the free acid and CoA, as opposed to long-chain acyl-CoA synthetases, which ligate fatty acids to CoA, to produce the CoA ester. The role of the ACOT- family of enzymes is not well understood; however, it has been suggested that they play a crucial role in regulating the intracellular levels of CoA esters, Coenzyme A, and free fatty acids. Recent studies have shown that Acyl-CoA esters have many more functions than simply an energy source. These functions include allosteric regulation of enzymes such as acetyl-CoA carboxylase, hexokinase IV, and the citrate condensing enzyme. Long-chain acyl-CoAs also regulate opening of ATP-sensitive potassium channels and activation of Calcium ATPases, thereby regulating insulin secretion. A number of other cellular events are also mediated via acyl-CoAs, for example signal transduction through protein kinase C, inhibition of retinoic acid-induced apoptosis, and involvement in budding and fusion of the endomembrane system. Acyl-CoAs also mediate protein targeting to various membranes and regulation of G Protein  subunits, because they are substrates for protein acylation. In the mitochondria, acyl-CoA esters are involved in the acylation of mitochondrial NAD+ dependent dehydrogenases; because these enzymes are responsible for amino acid catabolism, this acylation renders the whole process inactive. This mechanism may provide metabolic crosstalk and act to regulate the NADH/NAD+ ratio in order to maintain optimal mitochondrial beta oxidation of fatty acids. The role of CoA esters in lipid metabolism and numerous other intracellular processes are well defined, and thus it is hypothesized that ACOT- enzymes play a role in modulating the processes these metabolites are involved in.
ACTL6A
Actin-like protein 6A is a protein that in humans is encoded by the ACTL6A gene.

# Function
This gene encodes a family member of actin-related proteins (ARPs), which share significant amino acid sequence identity to conventional actins. Both actins and ARPs have an actin fold, which is an ATP-binding cleft, as a common feature. The ARPs are involved in diverse cellular processes, including vesicular transport, spindle orientation, nuclear migration and chromatin remodeling. This gene encodes a 53 kDa subunit protein of the BAF (BRG1/brm-associated factor) complex in mammals, which is functionally related to SWI/SNF complex in S. cerevisiae and Drosophila; the latter is thought to facilitate transcriptional activation of specific genes by antagonizing chromatin-mediated transcriptional repression. Together with beta-actin, it is required for maximal ATPase activity of BRG1, and for the association of the BAF complex with chromatin/matrix. Three transcript variants that encode two different protein isoforms have been described.

# Clinical significance
ACTL6A is amplified in head and squamous cancers and confers poor prognosis in patients. In hepatocellular carcinomas, it promotes metastasis.

# Interactions
ACTL6A has been shown to interact with SMARCA2, Myc, Transformation/transcription domain-associated protein, RuvB-like 1 and SMARCA4.
ACTR1A
Alpha-centractin (yeast) or ARP1 is a protein that in humans is encoded by the ACTR1A gene.

# Function
This gene encodes a 42.6 kD subunit of dynactin, a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein. It is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. This subunit is present in 8-13 copies per dynactin molecule, and is the most abundant molecule in the dynactin complex. It is an actin-related protein, and is approximately 60% identical at the amino acid level to conventional actin. ARP1 forms a 37 nm filament-like structure and is the core of the dynactin complex. It only exists in the dynactin complex in vivo. Highly purified, native Arp1 polymerize rapidly at extremely low concentrations into short filaments in vitro that were similar, but not identical, in length to those in dynactin. With time, these Arp1 filaments appeared to anneal to form longer assemblies but never attained the length of conventional actin filaments. As for conventional actin, Arp1 can bind and hydrolyze ATP, and Arp1 assembly is accompanied by nucleotide hydrolysis.
It has been reported that Arp1 interacts with other dynactin components including DCTN1/p150Glued,DCTN4/p62 and Actr10/Arp11. Arp1 has been shown as the domain for dynactin binding to membrane vesicles (such as Golgi or late endosome) through its association with -spectrin.

# Interactions
ACTR1A has been shown to interact with SPTBN2.
ACVR1B
Activin receptor type-1B is a protein that in humans is encoded by the ACVR1B gene.
ACVR1B or ALK-4 acts as a transducer of activin or activin like ligands (e.g., inhibin) signals.  Activin binds to either ACVR2A or ACVR2B and then forms a complex with ACVR1B. These go on to recruit the R-SMADs SMAD2 or SMAD3. ACVR1B also transduces signals of nodal, GDF-1, and Vg1; however, unlike activin, they require other coreceptor molecules such as the protein Cripto.

# Function
Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with a cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling, and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. This gene encodes activin A type IB receptor, composed of 11 exons. Alternative splicing and alternative polyadenylation result in 3 fully described transcript variants. The mRNA expression of variants 1, 2, and 3 is confirmed, and a potential fourth variant contains an alternative exon 8 and lacks exons 9 through 11, but its mRNA expression has not been confirmed.

# Interactions
ACVR1B has been shown to interact with
- ACVR2A, and ACVR2B
ACVR1C
The activin A receptor also known as ACVR1C or ALK-7 is a protein that in humans is encoded by the ACVR1C gene. ACVR1C is a type I receptor for the TGFB family of signaling molecules.
ACVR1C transduces signals of Nodal. Nodal binds to ACVR2B and then forms a complex with ACVR1C. These go on to recruit the R-SMADs SMAD2 or SMAD3.
Upon ligand binding, type I receptors phosphorylate cytoplasmic SMAD family transcription factors, which then translocate to the nucleus and interact directly with DNA or in complex with other transcription factors.