Persius/hicric huggingface dataset:
KIF1A
Kinesin-like protein KIF1A, also known as axonal transporter of synaptic vesicles or microtubule-based motor KIF1A, is a protein that in humans is encoded by the KIF1A gene.

# Function
KIF1A is a member of the kinesin family. This protein is highly similar to mouse heavy-chain kinesin member 1A protein, which is an anterograde motor protein that transports membranous organelles along axonal microtubules. It is thought that this protein may play a critical role in the development of axonal neuropathies resulting from impaired axonal transport. There are multiple polyadenylation sites found in this gene. Sexual orientation has been linked to the regulatory domain of the gene.

# Clinical significance
KIF1A is associated with hereditary spastic paraparesis.
The website KIF1A.org serves as a resource for patients and care-givers, and provides links to research efforts.
KIF22
Kinesin-like protein KIF22 is a protein that in humans is encoded by the KIF22 gene.
The protein encoded by this gene is a member of kinesin-like protein family. This family of proteins are microtubule-dependent molecular motors that transport organelles within cells and move chromosomes during cell division. The C-terminal half of this protein has been shown to bind DNA. Studies with the Xenopus homolog suggests an essential role in metaphase chromosome alignment and maintenance.

# Interactions
KIF22 has been shown to interact with SIAH1.

# Clinical relevance
Mutations in this gene have been shown to cause developmental disorders such as Spondyloepimetaphyseal dysplasia with joint laxity.
KIF23
Kinesin-like protein KIF23 is a protein that in humans is encoded by the KIF23 gene.

# Function

## In cell division
KIF23 (also known as Kinesin-6, CHO1/MKLP1, C. elegans ZEN-4 and Drosophila Pavarotti) is a member of kinesin-like protein family. This family includes microtubule-dependent molecular motors that transport organelles within cells and move chromosomes during cell division. This protein has been shown to cross-bridge antiparallel microtubules and drive microtubule movement in vitro. Alternate splicing of this gene results in two transcript variants encoding two different isoforms, better known as CHO1, the larger isoform and MKLP1, the smaller isoform.  KIF23 is a plus-end directed motor protein expressed in mitosis, involved in the formation of the cleavage furrow in late anaphase and in cytokinesis. KIF23 is part of the centralspindlin complex that includes PRC1, Aurora B and 14-3-3 which cluster together at the spindle midzone to enable anaphase in dividing cells.

## In neurons
In neuronal development KIF23 is involved in the transport of minus-end distal microtubules into dendrites and is expressed exclusively in cell bodies and dendrites.  Knockdown of KIF23 by antisense oligonucleotides and by siRNA both cause a significant increase in axon length and a decrease in dendritic phenotype in neuroblastoma cells and in rat neurons.  In differentiating neurons, KIF23 restricts the movement of short microtubules into axons by acting as a "brake" against the driving forces of cytoplasmic dynein. As neurons mature, KIF23 drives minus-end distal microtubules into nascent dendrites contributing to the multi-polar orientation of dendritic microtubules and the formation of their short, fat, tapering morphology.

# Interactions
KIF23 has been shown to interact with:
- ARF3,
- AURKB,
- BIRC6, and
- PRC1.

# Mutation and diseases
KIF23 has been implicated in the formation and proliferation of GL261 gliomas in mouse.
KIF3B
Kinesin-like protein KIF3B is a protein that in humans is encoded by the KIF3B gene.

# Function
The protein encoded by this gene forms a heterotrimeric motor complex with kinesin family member 3A and KAP3 (kinesin accessory protein 3) to drive intra-flagellar transport and possibly to aid in chromosome movement during mitosis and meiosis. The encoded protein is a plus end-directed microtubule motor and can interact with the SMC3 subunit of the cohesin complex. In addition, the encoded protein may be involved in the intracellular movement of membranous organelles. The heterotrimeric KIF3B/KIF3A/KAP3 motor protein is a member of the kinesin-2 subfamily of the kinesin superfamily.

# Interactions
KIF3B has been shown to interact with RAB4A.

# Model organisms
Model organisms have been used in the study of KIF3B function. A conditional knockout mouse line called Kif3btm1b(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed:  - In-depth immunological phenotyping
KLF13
Kruppel-like factor 13, also known as KLF13, is a protein that in humans is encoded by the KLF13 gene.
There is some evidence for KLF13 having a role in obesity.  A methylation site, cg07814318, within the first intron of KLF13 has been associated with obesity and orexigenic processes.  Ghrelin levels also positively correlated with methylation levels of cg07814318.  Moreover, expression levels of KLF13 were decreased and increased in the brains of starved and obese mice, respectively.

# Function
KLF13 belongs to a family of transcription factors that contain 3 classical zinc finger DNA-binding domains consisting of a zinc atom tetrahedrally coordinated by 2 cysteines and 2 histidines (C2H2 motif). These transcription factors bind to GC-rich sequences and related GT and CACCC boxes.
KLF13 was first described as the RANTES factor of late activated T lymphocytes (RFLAT)-1.  It regulates the expression of the chemokine RANTES in T lymphocytes.  It functions as a lynchpin, inducing a large enhancesome.  KLF13 knock-out mice show a defect in lymphocyte survival as KLF13 is a regulator of Bcl-xL expression.

# Interactions
KLF13 has been shown to interact with CREB-binding protein, Heat shock protein 47 and PCAF.
KLF14
Kruppel-like factor 14, also known as basic transcription element-binding protein 5 (BTEB5) is a protein that in humans is encoded by the KLF14 gene. The corresponding Klf14 mouse gene is known as Sp6.

# Function
KLF14 is a member of the Kruppel-like factor family of transcription factors.  It regulates the transcription of various genes, including TGFRII (the type II receptor for TGF). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression.
KLF14 appears to be a master regulator of gene expression in adipose tissue.

# Protein structure
Like the other members of the KLF family, KLF14 has three zinc-finger domains near the C-terminus, all three of which are of the classical C2H2 type.  In the human, they are at amino acids 195219, 225249, and 255277.
Human KLF14 is 323 amino acids in length, with a molecular weight of 33,124; in the mouse its length is 325.

# Clinical significance
There appears to be a connection between KLF14 and coronary artery disease, hypercholesterolemia and type 2 diabetes.
KLRC2
NKG2-C type II integral membrane protein is a protein that in humans is encoded by the KLRC2 gene.

# Function
Natural killer (NK) cells are lymphocytes that can mediate lysis of certain tumor cells and virus-infected cells without previous activation. They can also regulate specific humoral and cell-mediated immunity. NK cells preferentially express several calcium-dependent (C-type) lectins, which have been implicated in the regulation of NK cell function. The group, designated KLRC (NKG2) are expressed primarily in natural killer (NK) cells and encodes a family of transmembrane proteins characterized by a type II membrane orientation (extracellular C terminus) and the presence of a C-type lectin domain. The KLRC (NKG2) gene family is located within the NK complex, a region that contains several C-type lectin genes preferentially expressed on NK cells. KLRC2 alternative splice variants have been described but their full-length nature has not been determined.

# Interactions
KLRC2 has been shown to interact with KLRD1.
The binding of this CD94/NKG2C heterodimer to its cellular ligand HLA-E has been shown to drive the expansion of a subset of Natural Killer (NK) cells in response to viral infections.
KLRD1
CD94 (Cluster of Differentiation 94), also known as killer cell lectin-like receptor subfamily D, member 1 (KLRD1) is a human gene.
The protein encoded by CD94 gene is a lectin, cluster of differentiation and a receptor that is involved in cell signaling and is expressed on the surface of natural killer cells in the innate immune system.  CD94 pairs with the NKG2 molecule as a heterodimer.  The CD94/NKG2 complex, on the surface of natural killer cells interacts with Human Leukocyte Antigen (HLA)-E on target cells.

# Function
Natural killer (NK) cells are a distinct lineage of lymphocytes that mediate cytotoxic activity and secrete cytokines upon immune stimulation. Several genes of the C-type lectin superfamily, including members of the NKG2 family, are expressed by NK cells and may be involved in the regulation of NK cell function. KLRD1 (CD94) is an antigen preferentially expressed on NK cells and is classified as a type II membrane protein because it has an external C terminus. KLRD1 has two alternatively spliced variants that differ in the presence or absence of exon 2 sequence.

# Interactions
KLRD1 has been shown to interact with KLRC2.
KLRG1
Killer cell lectin-like receptor subfamily G member 1 is a protein that in humans is encoded by the KLRG1 gene.

# Function
Natural killer (NK) cells are lymphocytes that can mediate lysis of certain tumor cells and virus-infected cells without previous activation. They can also regulate specific humoral and cell-mediated immunity. The protein encoded by this gene belongs to the killer cell lectin-like receptor (KLR) family, which is a group of transmembrane proteins preferentially expressed in NK cells. Studies in mice suggested that the expression of this gene may be regulated by MHC class I molecules.
KLRG1 is a lymphocyte co-inhibitory, or immune checkpoint, receptor expressed predominantly on late-differentiated effector and effector memory CD8+ T and NK cells. Its ligands are E-cadherin and N-cadherin with similar affinities, respective markers of epithelial and mesenchymal cells. Targeting of other co-inhibitory receptors for applications in oncology has gained widespread interest (e.g., CTLA-4, PD-1, and its ligand PD-L1). Unlike the obvious enhanced immune activation present in CTLA-4 and PD-1 gene knockout mice,  KLRG1 knockout mice initially were found to have no abnormal features, though were subsequently found to have enhanced immunity in a tuberculosis challenge model.
The characterization of KLRG1 as a senescent marker, but other co-inhibitory receptors as exhaustion markers, has contributed to relatively fewer studies on this molecule.
KRT31
Keratin, type I cuticular Ha1 is a protein that in humans is encoded by the KRT31 gene.

# Function
The protein encoded by this gene is a member of the keratin gene family. As a type I hair keratin, it is an acidic protein which heterodimerizes with type II keratins to form hair and nails. The type I hair keratins are clustered in a region of chromosome 17q12-q21 and have the same direction of transcription.

# Model organisms
Model organisms have been used in the study of KRT31 function. A conditional knockout mouse line called Krt31tm1e(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed:  - In-depth immunological phenotyping
KRT71
KRT71 is a keratin gene. Keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are
subdivided into epithelial keratins and hair keratins. This gene encodes a protein that is expressed in the inner
root sheath of hair follicles. The type II keratins are clustered in a region of chromosome 12q13.(provided by
RefSeq, Jun 2009)
Kampo
Kampo (or Kanpo, ) medicine is the Japanese study and adaptation of Traditional Chinese medicine. The basic works of Chinese medicine came to Japan between the 7th and 9th centuries.  Since then, the Japanese have created their own unique herbal medical system and diagnosis.  Kampo uses most of the Chinese medical system including acupuncture and moxibustion but is primarily concerned with the study of herbs.

# Approved Kampo medicines
Today in Japan, Kampo is integrated into the national health care system. In 1967, the  Ministry of Health, Labour and Welfare approved four kampo medicines for reimbursement under the National Health Insurance (NHI) program. In 1976, 82 kampo medicines were approved by the  Ministry of Health, Labour and Welfare. Currently, 148 kampo medicines are approved for reimbursement.
Rather than modifying formulae as in Traditional Chinese medicine, the Japanese kampo tradition uses fixed combinations of herbs in standardized proportions according to the classical literature of Chinese medicine. Kampo medicines are produced by various manufacturers. However, each medicine is composed of exactly the same ingredients under the  Ministry's standardization methodology. The medicines are therefore prepared under strict manufacturing conditions that rival pharmaceutical companies. The two leading companies making kampo medicines are Tsumura () and Kanebo ().
Extensive modern scientific research in Japan has validated the effectiveness of kampo medicines. In October 2000, a nationwide study reported that 72% of registered physicians prescribe kampo medicines.

# Herbs used in kampo medicines
The 14th edition of the Japanese Pharmacopoeia (JP) ( Nihon yakkyokuho) lists 165 herbal ingredients that are used in kampo medicines.
Tsumura () is the leading maker of kampo medicine. They make 128 of the 148 kampo medicines. The most common herb in kampo medicine is Glycyrrhizae Radix (Chinese liquorice root). It is in 94 of the 128 Tsumura formulae. Other common herbs are Zingiberis Rhizoma (ginger) (51 of 128 formulae) and Paeoniae Radix (Chinese peony root) (44 of 128 formulae).

# Kampo outside Japan
In the United States, kampo is practiced mostly by acupuncturists, Chinese medicine practitioners, naturopath physicians, and other alternative medicine professionals. Kampo herbal formulae are studied under clinical trials, such as the clinical study of Sho-saiko-to (H09) for treatment of hepatitis C at New York Memorial Sloan-Kettering Cancer Center and liver cirrhosis caused by hepatitis C at UCSD Liver Center. Both clinical trials are sponsored by Honso USA, Inc., a branch of Honso Pharmaceutical Co., Ltd., Nagoya, Japan.
Katal
The katal (symbol: kat) is the SI unit of catalytic activity. It is a derived SI unit for expressing quantity values of catalytic activity of enzymes and other catalysts. Its use is recommended by the General Conference on Weights and Measures and other international organizations. It replaces the non-SI enzyme unit. Enzyme units are, however, still more commonly used than the katal in practice at present, especially in biochemistry.
The katal is not used to express the rate of a reaction; that is expressed in moles per second. Rather, it is used to express catalytic activity which is a property of the catalyst. The katal is invariant of the measurement procedure, but the numerical quantity value is not and depends on the experimental conditions. Therefore, in order to define the quantity of a catalyst, the rate of conversion of a defined chemical reaction has to be specified, preferably of the first order, under strictly controlled conditions. One katal of trypsin, for example, is that amount of trypsin which breaks a mole of peptide bonds per second under specified conditions.

# Definition
 kat =  mol/s 

# SI multiples

# Origin
The name katal has been used for decades and it became an official SI unit in 1999.
Kvass
Kvass (literally "leaven"; borrowed in the 16th century from Russian ), sometimes translated into English as bread drink, is a fermented mildly alcoholic beverage made from black or rye bread. It is popular in Russia, Belarus, Ukraine and other Eastern and Central European countries as well as in all ex-Soviet states, like Uzbekistan, where one can see many kvass vendors in the streets.
The alcohol content is so low (0.05-1.44%) that it is considered acceptable for consumption by children. It is often flavoured with fruits or herbs such as strawberries or mint. Russians also use kvass for cooking a special summer cold soup, okroshka.

# History
Kvass has been a common drink in Eastern Europe since ancient times. It was at first mentioned in old-russian chronicles under 989. It has been both a commercial product and homemade. It used to be consumed widely in most Slavic countries, and in almost every city there are kvass vendors on the street.

# Manufacturing
Kvass is made by the natural fermentation of bread made from wheat, rye, or barley, and sometimes flavoured with fruit, berries, raisins or birch sap collected in the early spring.
Modern homemade kvass most often uses black or rye bread, usually dried, baked into croutons (called suharki), or fried, with the addition of sugar or fruit (e.g. apples or raisins), and with a yeast culture and zakvasska ("kvass fermentation starter").
Commercial kvass is often made just like any other soft drink using sugar, carbonated water, malt extract and flavourings. Kvass is commonly served unfiltered, with the yeast still in it, which adds to its unique flavour as well as its high vitamin B content.

# Variant names
- Russian, Belarusian, Serbian and Ukrainian:  (kvas);
- Polish: kwas chlebowy (lit. "bread leaven"),
- Lithuanian: gira;
- Estonian: kali.

## Kvass in Latvia
After the fall of the Soviet Union in 1991, the street vendors disappeared from the streets of Latvia due to new health laws that banned its sale on the street and economic disruptions forced many kvass factories to close. The Coca-Cola company moved in and quickly dominated the market for soft drinks, but in 1998 the local soft drink industry fought back by selling bottled kvass and launching an aggressive marketing campaign. This surge was further stimulated by the fact that kvass sold for about half the price of Coca-Cola. In just three years, kvass constituted as much as 30% of the soft drink market in Latvia, while the market share of Coca-Cola fell from 65% to 44%. The Coca-Cola company had losses in Latvia of about $1 million in 1999 and 2000. The situation was similar in the other Baltic countries and in Russia. Coca-Cola fought back by buying kvass manufacturers and also started making kvass at their soft drink plants.

# Similar beverages
Other beverages from around the world that are traditionally low-alcohol and lacto-fermented include:
- Kombucha
- Chicha
- Ibwatu
- Pulque
- Toddy
- Malta
LACTB
Serine beta-lactamase-like protein LACTB, mitochondrial is an enzyme that in humans is encoded by the LACTB gene. This gene encodes a 54 kDa protein sharing significant 
sequence similarity to serine proteases of the penicillin binding protein and beta-lactamase superfamily occurring in bacteria.
 It is involved in the regulation of the metabolic circuitry. A causal association has been found between LACTB and obesity.  In breast cancer, LACTB has a tumor suppressor function by modulating lipid metabolism.

# Structure

## Gene
The LACTB gene is located at chromosome 15q22.1, consisting of 8 exons. Alternative splicing results in multiple transcript variants encoding different protein isoforms.

## Protein
LACTB shares sequence similarity to the beta-lactamase/penicillin-binding protein family of serine proteases that are involved in bacterial cell wall metabolism. The N-terminal 97 amino acid segment of LACTB does not form part of the conserved penicillin-binding protein domain and may therefore be responsible for organelle targeting. 

# Function
LACTB is widely expressed in different mammalian tissues, with the predominant expression in human skeletal muscle. It localizes in the mitochondrial intermembrane space.  LACTB can polymerize into stable filaments occupying the mitochondrial intermembrane space. These filaments are speculated to play a role in submitochondrial organization and therefore possibly affect mitochondrial metabolon organization. 

# Clinical significance
It has been found LACTB could cause obesity through gene co-expression analysis based on data integrated from multiple sources. This has been validated in vivo through LACTB overexpression in transgenic mice, which resulted in an obese phenotype. LACTB has also been identified to be a tumor suppressor through its effect on mitochondrial phospholipid metabolism and modulation of cell differentiation state.

# Interactions
- MiR-125b-5p
LAMP3
Lysosome-associated membrane glycoprotein 3 (LAMP3, Lamp3) is a protein that in humans is encoded by the LAMP3 gene. It is one of the lysosome-associated membrane glycoproteins.
LAMP3 also known as DC-LAMP (Dendritic cell lysosomal associated membrane glycoprotein) is a member of the LAMP family along with LAMP1 and LAMP2, these proteins make up the members of the glycoconjugate coat present on the inside of the lysosomal membrane. In humans, this protein is almost exclusively found in mature Dendritic cells. While LAMP3 can be observed on the surface of dendritic cells, the protein is mainly found within lysosomes. LAMP3 first appears in the MHC Class II compartment and in cells aids in the identifying and processing of an antigen during an immune response. LAMP3 protein is linked with the maturation of dendritic cells, and as a marker for transformed type II pneumocytes or alveolar cells.
Studies have linked LAMP3 with the inhibition of the viral replication of Influenza A cells.

# Structure and Tissue Distribution
LAMP3 is a Type I integral membrane protein consisting of about 416 amino acid residues with about 90% of the protein located within the lumen of the lysosomes. LAMP3 has been shown to be highly expressed in dendritic cells during cell differentiation and maturation. During human fetal development, between weeks 10 and 20, LAMP3 is highly expressed in the lungs, while in normal adult tissue cells LAMP3 is expressed in the lungs, appendix, testis and lymph nodes.
LARGE
Glycosyltransferase-like protein LARGE1 is an enzyme that in humans is encoded by the LARGE gene.

# Function
This gene, which is one of the largest in the human genome, encodes a member of the N-acetylglucosaminyltransferase gene family. The exact function of LARGE, a golgi protein, remains uncertain. It encodes a glycosyltransferase which participates in glycosylation of alpha-dystroglycan, and may carry out the synthesis of glycoprotein and glycosphingolipid sugar chains. It may also be involved in the addition of a repeated disaccharide unit. Mutations in this gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan. Alternative splicing of this gene results in two transcript variants that encode the same protein.
LARGE may also play a role in tumor-specific genomic rearrangements. Mutations in this gene may be involved in the development and progression of meningioma through modification of ganglioside composition and other glycosylated molecules in tumor cells.