Persius/hicric huggingface dataset:
LRRC8C
Leucine-rich repeat-containing protein 8C is a protein that in humans is encoded by the LRRC8C gene. Researchers have found out that this protein, along with the other LRRC8 proteins LRRC8A, LRRC8B, LRRC8D, and LRRC8E, is sometimes a subunit of the heteromer protein Volume-Regulated Anion Channel. Volume-Regulated Anion Channels (VRACs) are crucial to the regulation of cell size by transporting chloride ions and various organic osmolytes, such as taurine or glutamate, across the plasma membrane, and that is not the only function these channels have been linked to.
While LRRC8C is one of many proteins that can be part of VRAC, research has found that it is not as crucial to the activity of the channel in comparison to LRRC8A and LRRC8D. However, while we know that LRRC8A and LRRC8D are necessary for VRAC function, other studies have found that they are not sufficient for the full range of usual VRAC activity. This is where the other LRRC8 proteins come in, such as LRRC8C, as the different composition of these subunits affects the range of specificity for VRACs.
In addition to its role in VRACs, the LRRC8 protein family is also associated with agammaglobulinemia-5.
LRRC8D
Leucine-rich repeat-containing protein 8D is a protein that in humans is encoded by the LRRC8D gene. Researchers have found out that this protein, along with the other LRRC8 proteins LRRC8A, LRRC8B, LRRC8C, and LRRC8E, is a subunit of the heteromer protein Volume-Regulated Anion Channel. Volume-Regulated Anion Channels (VRACs) are crucial to the regulation of cell size by transporting chloride ions and various organic osmolytes, such as taurine or glutamate, across the plasma membrane, and that is not the only function these channels have been linked to.
While LRRC8D is one of many proteins that can be part of VRAC, it is in fact one of the most important subunits for the channels ability to function; the other protein of importance is LRRC8A.  However, while we know it is necessary for specific VRAC function, other studies have found that it is not sufficient for the full range of usual VRAC activity. This is where the other LRRC8 proteins come in, as the different composition of these subunits affects the range of specificity for VRACs.
In addition to its role in VRACs, the LRRC8 protein family is also associated with agammaglobulinemia-5.
LRRC8E
Leucine-rich repeat-containing protein 8E is a protein that in humans is encoded by the LRRC8E gene. Researchers have found out that this protein, along with the other LRRC8 proteins LRRC8A, LRRC8B, LRRC8C, and LRRC8D, is sometimes a subunit of the heteromer protein Volume-Regulated Anion Channel. Volume-Regulated Anion Channels (VRACs) are crucial to the regulation of cell size by transporting chloride ions and various organic osmolytes, such as taurine or glutamate, across the plasma membrane, and that is not the only function these channels have been linked to.
While LRRC8E is one of many proteins that can be part of VRAC, research has found that it is not as crucial to the activity of the channel in comparison to LRRC8A and LRRC8D. However, while we know that LRRC8A and LRRC8D are necessary for VRAC function, other studies have found that they are not sufficient for the full range of usual VRAC activity. This is where the other LRRC8 proteins come in, such as LRRC8E, as the different composition of these subunits affects the range of specificity for VRACs.
In addition to its role in VRACs, the LRRC8 protein family is also associated with agammaglobulinemia-5.
Specifically for LRRC8E, there has been a recent study that found that this gene was nominally associated with panic disorder.
LRRIQ3
LRRIQ3 (Leucine-rich repeats and IQ motif containing 3), which is also known as LRRC44, is a protein that in humans is encoded by the LRRIQ3 gene. It is predominantly expressed in the testes, and is linked to a number of diseases.

# Gene

## Locus
LRRIQ3 is found on the minus strand of the end of the short arm of human chromosome 1 at 1p31.1.

## Overall Structure
There are a total of 7 exons in the putative sequence of LRRIQ3.

# mRNA

## Expression
LRRIQ3 is expressed as 2 primary isoforms, which produce proteins of length 624 amino acids and 464 amino acids respectively. It is expressed at low levels in human and brown rat tissues, with highest expression levels in testes tissue. There are relatively high expression levels in T cells, the epididymis, the kidney, and a number of glands.

# Protein

## General Characteristics and Compositional Features
Human protein LRRIQ3 Isoform 1 consists of 624 amino acids, and has a molecular weight of 73.7 kDa. The isoelectric point of LRRIQ3 is 9.73, which suggests that LRRIQ3 is basic at normal physiological pH (~7.4). Additionally, there is strong evidence that human LRRIQ3 localizes to the plasma membrane from antibody staining. LRRIQ3 is rich in lysine residues, with a total of 82 lysines. It is also slightly low on glycines.

## Domains and Motifs
In total, there are 4 conserved domains within LRRIQ3: 3 leucine-rich repeats and 1 IQ calmodulin-binding motif. Leucine-rich repeats are typically involved in protein-protein interactions, and form a characteristic / horseshoe fold. An IQ motif provides a binding site for calmodulin (CaM) or CaM-like proteins.

## Secondary and Tertiary Structure
LRRIQ3 is predicted to be mostly alpha-helical in structure, including a long alpha-helical C-terminal domain. It is also predicted to function as a monomer.

## Post-translational Modifications
LRRIQ3 is predicted to undergo many post-translational modifications. These include O-GlcNAcylation, SUMOylation, ubiquitination, and phosphorylation. LRRIQ3 is predicted to have 4 well conserved SUMOlyation sites and 1 well conserved ubiquitination site. A representation of these post-translational modifications is shown in the figure below.

## Protein Interactions
There is evidence that LRRIQ3 interacts with a number of proteins from two-hybrid assays and affinity chromatography. The proteins LRRIQ3 interact with include LYN,  NCK2, GNB4, and ABL1. These proteins are associated with cell signalling, cytoskeletal reorganization, and cell differentiation, as well as others.

# Homology and evolution

## Paralogs and Orthologs
No paralogs exists for LRRIQ3 in humans. However, there are a number of orthologs, as reported by BLAST, some of which are listed below. The number of years since divergence from the human protein, listed in "million of years ago (MYA)" below, were calculated using TimeTree.

# Clinical significance
LRRIQ3 is linked to a number of cancers. RNA-seq experiments have shown that LRRIQ3 is severely down-regulated (Log2-fold changes between -3.4 and -4.2) in a number of disease states, including pancreatic cancer, colorectal cancer, and breast cancer.
LRRTM1
LRRTM1 is a brain-expressed imprinted gene that encodes a leucine-rich repeat transmembrane protein that interacts with neurexins and neuroligins to modulate synaptic cell adhesion in neurons. As the name implies, its protein product is a transmembrane protein that contains many leucine rich repeats.  It is expressed during the development of specific forebrain structures and shows a variable pattern of maternal downregulation (genomic imprinting).

# Clinical significance
LRRTM1 is the first gene linked to increased odds of being left-handed, when inherited from the father's side. Possessing one particular variant of the LRRTM1 gene slightly raises the risk of psychotic mental illnesses such as schizophrenia, again only if inherited from the father's side. As well, LRRTM1 has been associated with measures of schizotypy in non-clinical populations, indicating that the gene may have shared effects on neurodevelopment in both healthy and unhealthy individuals and individuals with schizophrenia.
LRRTM1 is also critically involved in synapse formation within the dorsal Lateral geniculate nucleus (dLGN) of mice. LRRTM1 aids in the assembly of complex retinogenciulate synapses in mice, which are believed to help process complex visual signals. Lack of this gene shows decreased performance in complex visual tasks.
LRTOMT
Leucine rich transmembrane and O-methyltransferase domain containing is a protein that in humans is encoded by the LRTOMT gene.

# Clinical significance
Mutations in LRTOMT are associated to                 non syndromic deafness            .

# Function
This gene includes two transcript forms. The short form has one open reading frame (ORF), which encodes the leucine-rich repeats (LRR)-containing protein of unknown function. This protein is called LRTOMT1 or LRRC51. The long form has two alternative ORFs; the upstream ORF has the same translation start codon as used in the short form and the resulting transcript is a candidate for nonsense-mediated decay, and the downstream ORF encodes a different protein, which is a transmembrane catechol-O-methyltransferase and is called LRTOMT2, TOMT or COMT2. The COMT2 is essential for auditory and vestibular function. Defects in the COMT2 can cause nonsyndromic deafness. Alternatively spliced transcript variants from each transcript form have been found for this gene.
Labium

# Overview
Labium (plural labia) is a Latin-derived term meaning "Lip".  Labium and its derivatives (including labial, labrum) are used to describe any lip-like structure, but in the English language, labium often specifically refers to parts of the vulva.

# Anatomy
The labia majora are lip-like structures comprised mostly of skin and adipose tissue, which extend on either side of the vulva, and after puberty are naturally covered with pubic hair. When standing or with the legs together, they usually entirely or partially cover the other parts of the vulva.
The labia minora (obsolete: nymphae) are two soft folds of skin within the labia majora and to either side of the opening of the vagina. The clitoris is anterior to the vulva where the labia minora meet superiorly. The visible tip of the clitoris, the clitoral glans, is entirely or partially covered by a "hood" of tissue (the clitoral hood).
The coloration, size and general appearance of the labia can vary extensively from woman to woman.  In some women the labia minora are almost non-existent, and in others they can be fleshy and protuberant. It is not uncommon for them to be asymmetrical. Some differences are purely personal, while others may be genetically linked; a striking example of the latter being the elongated labia minora of the Khoisan peoples, whose "khoikhoi aprons" can hang down up to four inches past their labia majora when they are standing.
During sexual arousal, the labia become engorged with blood, typically swelling slightly and darkening or reddening in color.
Labiaplasty is a controversial plastic surgery procedure that involves the creation or reshaping of the labia.

# Additional images
- Outer anatomy of clitoris.
- Organs of the female reproductive system.
- Sagittal section of the lower part of a female trunk, right segment.
- Median sagittal section of female pelvis.
Lactam
A lactam (the noun is a portmanteau of the words lactone + amide) is a cyclic amide. Prefixes may indicate the ring size: -lactam (4-membered), -lactam (5-membered), -lactam (6-membered ring). That order in the nomenclature is because beta , gamma  and delta  are the second, third and fourth letters in the alphabetical order of the Greek alphabet, respectively.

# Synthesis
General synthetic methods exist for the organic synthesis of lactams.
- Lactams form by the acid-catalyzed rearrangement of oximes in the Beckmann rearrangement.
- Lactams form from cyclic ketones and ammonia in the Schmidt reaction.
- lactams form from cyclisation of amino acids.
- In iodolactamization  an iminium ion reacts with an halonium ion formed in situ by reaction of an alkene with iodine.
- Lactams form by copper catalyzed 1,3-dipolar cycloaddition of alkynes and nitrones in the Kinugasa reaction

# Reactions
- Lactams can polymerize to polyamides.
Lesion

# Overview
Lesion is derived from the Latin word  "laesio" which means "injury."
A lesion is any abnormal tissue found on or in an organism, usually damaged by disease or trauma.

# Causes of lesions
Lesions are caused by any process that damages tissues.  A cancerous tumor is an example of a lesion, however the surrounding tissue damaged by a tumour is also a lesion.  Trauma, including electrocution and chemical burns cause lesions.  Certain diseases present lesions, for example the skin deformities caused by chicken pox.  Lesions can also be caused by metabolic processes, like an ulcer or autoimmune activity, as in the case with many forms of arthritis.
Lesions are sometimes intentionally inflicted during neurosurgery, such as the carefully-placed brain lesion used to treat epilepsy and other brain disorders.
Note that lesions are not limited to animals or humans; damaged plants are said to have lesions.

# Types of lesions
Because the definition of lesion is so broad, the varieties of lesions are virtually endless. They are subsequently classified by their features.  If a lesion is caused by cancer it will be classified as malignant versus benign.  They may be classified by the shape they form, as is the case with many ulcers which appear like as a bullseye or 'target'.  Their size may be specified as gross or histologic depending on if they are visible to the unaided eye or if they require a microscope to see.
An additional classification that is sometimes used is based on whether or not a lesion occupies space. A space occupying lesion, as the name suggests, occupies space and may impinge on nearby structures, whereas a non space occupying lesion is simply a hole in the tissue, e.g. a small area of the brain that has turned to fluid following a stroke.
Some lesions have specialized names, like the Gohn lesions in the lungs of tuberculosis victims.  The characteristic skin lesions of a varicella-zoster virus infection are called chickenpox.  Lesion of the teeth are usually called dental caries.
Finally, they are often classified by their location.  For example, compare a 'skin lesion' versus a 'brain lesion'.
Ligase

# Overview
In biochemistry, a ligase (from the Latin verb ligare  "to bind" or "to glue together") is an enzyme that can catalyse the joining of two large molecules by forming a new chemical bond, usually with accompanying hydrolysis of a small chemical group pendant to one of the larger molecules. Generally ligase catalyses the following reaction:
-r sometimes
where the lower case letters signify the small, pendant groups.

# Nomenclature
The common names of ligase enzymes often include the word "ligase", such as DNA ligase, an enzyme commonly used in molecular biology laboratories to join together DNA fragments. Other common names for ligases include synthetase, because they are used to synthesize new molecules, or carboxylase when they are used to add carbon dioxide to a molecule.
Note that "synthetase" should not be confused with synthases, as synthases do not use adenosine triphosphate and belong to the lyase group, while synthetases do use adenosine triphosphate (ATP).

# Classification
Ligases are classified as EC 6 in the EC number classification of enzymes. Ligases can be further classified into six subclasses:
- EC 6.1 includes ligases used to form carbon-oxygen bonds
- EC 6.2 includes ligases used to form carbon-sulfur bonds
- EC 6.3 includes ligases used to form carbon-nitrogen bonds (including argininosuccinate synthetase)
- EC 6.4 includes ligases used to form carbon-carbon bonds
- EC 6.5 includes ligases used to form phosphoric ester bonds
- EC 6.6 includes ligases used to form nitrogen-metal bonds
Lochia

# Overview
In the field of obstetrics, lochia is post-partum vaginal discharge, containing blood, mucus, and placental tissue. Lochia discharge typically continues for 4 to 6 weeks after childbirth and progresses through three stages.

# Types of Lochia
Lochia rubra is the first discharge, red in color because of the large amount of blood it contains. It typically lasts no longer than 3 to 5 days after birth.
Lochia serosa is the term for lochia which has thinned and turned brownish or pink in color. It contains serous exudate, erythrocytes, leukocytes, and cervical mucus. This stage continues until around the tenth day after delivery.
Lochia alba is the name for lochia once it has turned whitish or yellowish-white. It typically lasts from the second through the third to sixth week after delivery. It contains fewer red blood cells and is mainly made up of leukocytes, epithelial cells, cholesterol, fat, and mucus.

# Characteristics
Lochia generally has an odor similar to that of normal menstrual fluid. Any offensive odor indicates a possible infection and should be reported to a healthcare provider.
de:Wochenfluss
Lunate
The lunate bone (semilunar bone) is a bone in the human hand that may be distinguished by its deep concavity and crescentic outline. It is situated in the center of the proximal row of the carpus, or wrist, between the scaphoid and triangular bone.
The etymology derives from the Latin luna which means "moon."

# Surfaces
The superior surface, convex and smooth, articulates with the radius.
The inferior surface is deeply concave, and of greater extent from before backward than transversely: it articulates with the head of the capitate, and, by a long, narrow facet (separated by a ridge from the general surface), with the hamate.
The dorsal and palmar surfaces are rough, for the attachment of ligaments, the former being the broader, and of a somewhat rounded form.
The lateral surface presents a narrow, flattened, semilunar facet for articulation with the scaphoid.
The medial surface is marked by a smooth, quadrilateral facet, for articulation with the triangular bone.
MAD1L1
Mitotic spindle assembly checkpoint protein MAD1 is a protein that in humans is encoded by the MAD1L1 gene.
MAD1L1 is also known as Human Accelerated Region 3.  It may therefore have played a key role in differentiating Humans from Apes.

# Function
MAD1L1 is a component of the mitotic spindle-assembly checkpoint that prevents the onset of anaphase until all chromosome are properly aligned at the metaphase plate. MAD1L1 functions as a homodimer and interacts with MAD2L1. MAD1L1 may play a role in cell cycle control and tumor suppression. Three transcript variants encoding the same protein have been found for this gene.

# Interactions
MAD1L1 has been shown to interact with:
- HDAC1,
- Histone deacetylase 2, and
- MAD2L1,
MAGEA3
Melanoma-associated antigen 3 (MAGE-A3) is a protein that in humans is encoded by the MAGEA3 gene.

# Genetics
This gene is a member of the melanoma-associated antigen gene family. The members of this family encode proteins with 50 to 80% sequence identity to each other. The promoters and first exons of the MAGEA genes show considerable variability, suggesting that the existence of this gene family enables the same function to be expressed under different transcriptional controls. The MAGEA genes are clustered at chromosomal location Xq28. They have been implicated in some hereditary disorders, such as dyskeratosis congenita.

# Function and Clinical relevance
The normal function of MAGE-A3 in healthy cells is unknown. The presence of the antigen on tumor cells has been associated with worse prognosis. In one study, high levels of MAGE-A3 in lung adenocarcinoma were associated with shorter survival.
MAGE-A3 is a tumor-specific protein, and has been identified on many tumors including melanoma, non-small cell lung cancer, hematologic malignancies, among others. Currently, GlaxoSmithKline is developing a cancer vaccine targeting MAGE-A3.  The vaccine is a fusion protein of MAGE-A3 and Haemophilus influenzae protein D, combined with a proprietary immunoadjuvant.
MAGED1
Melanoma-associated antigen D1 is a protein that in humans is encoded by the MAGED1 gene.

# Function
This gene is a member of the melanoma antigen gene (MAGE) family. Most of the genes of this family encode tumor specific antigens that are not expressed in normal adult tissues except testis. Although the protein encoded by this gene shares strong homology with members of the MAGE family, it is expressed in almost all normal adult tissues. This gene has been demonstrated to be involved in the p75 neurotrophin receptor mediated programmed cell death pathway. Three transcript variants encoding two different isoforms have been found for this gene.
MAGED was found to be deleted in a group of children with an intellectual disability disorder caused by a Xp11.22 deletion.
Maged1 plays a role in controlling the reward circuitry in the brain of mice that is responsible for addictive behaviors.

# Interactions
MAGED1 has been shown to interact with UNC5A, PJA1 and XIAP.
MAGEH1
Melanoma-associated antigen H1 is a protein that in humans is encoded by the MAGEH1 gene.
This gene is thought to be involved in apoptosis. Multiple polyadenylation sites have been found for this gene.

# Interactions
MAGEH1 has been shown to interact with Low affinity nerve growth factor receptor.
MALAT1
MALAT 1 (metastasis associated lung adenocarcinoma transcript 1) also known as NEAT2 (noncoding nuclear-enriched abundant transcript 2) is a large, infrequently spliced non-coding RNA, which is highly conserved amongst mammals and highly expressed in the nucleus. MALAT1 was identified in multiple types of physiological processes, such as alternative splicing, nuclear organization, epigenetic modulating of gene expression, and a number of evidences indicate that MALAT1 also closely relate to various pathological processes, ranging from diabetes complications to cancers.  It regulates the expression of metastasis-associated genes.  It also positively regulates cell motility via the transcriptional and/or post-transcriptional regulation of motility-related genes. MALAT1 may play a role in temperature-dependent sex determination in the Red-eared slider turtle (Trachemys scripta).

# Expression in alcoholic brains
Transcripts of MALAT1 are significantly increased in the cerebellum of human alcoholics, as well as in similar regions of rat brains after the withdrawal of ethanol vapours. This alcohol-induced upregulation of MALAT1 may be responsible for differential expression of a number of proteins which contribute to ethanol tolerance and dependency in humans.

# Prognostic potential in cancer
The implication of MALAT1 RNA in the pathology of various cancers has been documented.  Elevated MALAT1 expression is correlated with poor overall survival in various types of cancer, suggesting that this gene is a prognostic factor for different types of cancer.

# As a target for the treatment of cancer
Genetic loss or systemic knockdown of Malat1 using antisense oligonucleotides (ASO) in the mouse mammary carcinoma model results in slower tumor growth accompanied by significant differentiation into cystic tumors and a reduction in metastasis. At the molecular level, the ASO-Malat1 hybrid stimulates a naturally occurring cellular enzyme that degrades the Malat1 lncRNA. Malat1 knockdown results in alterations in gene expression and changes in splicing patterns of genes involved in differentiation and protumorigenic signaling pathways. Metastatic tumors have a dependency on Malat1they can't thrive without it. And very importantly, only the cancer cells seem to require it. In so far as MALAT1 has been identified to be involved in tumorigenesis of various types of cancer such as lung cancer, pancreatic cancer, cervical cancer Malat1 ASOs represent a potential therapy for inhibiting such cancers progression.