Persius/hicric huggingface dataset:
NLRP1
NACHT, LRR and PYD domains-containing protein 1 is a protein that in humans is encoded by the NLRP1 gene.

# Function
This gene encodes a member of the Ced-4 family of apoptosis proteins. Ced-family members contain a caspase recruitment domain (CARD) and are known to be key mediators of programmed cell death. The encoded protein contains a distinct N-terminal pyrin-like motif, which is possibly involved in protein-protein interactions. The NLRP1 protein interacts strongly with caspase 2 and weakly with caspase 9. Overexpression of this gene was demonstrated to induce apoptosis in cells. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene, but the biological validity of some variants has not been determined.

# Interactions
NLRP1 has been shown to interact with caspase 9 and APAF1.
NLRX1
NLRX1 or NLR family member X1, short for nucleotide-binding oligomerization domain, leucine rich repeat containing X1 is a protein that in humans is encoded by the NLRX1 gene.  It is also known as NOD-like receptor X1, NLR family, X1, NOD5, NOD9, and CLR11.3, and is a member of the NOD-like receptor family of pattern recognition receptors.

# Function
NLRX1 is an intracellular protein that plays a role in the immune system.  NLRX1 has been proposed to affect innate immunity to viruses by interfering with the mitochondrial antiviral signaling protein (MAVS)/retinoic-acid-inducible gene I (RIG-I) mitochondrial antiviral pathway., although this was recently questioned.
NLRX1 also plays a role in host immunity during bacterial infections, such as Chlamydia trachomatis and Helicobacter pylori, by regulating bacterial burden and inflammation in mononuclear phagocytes. Mechanisms underlying the modulation of NLRX1 are not well characterized, however computational modeling predictions suggest that levels of NLRX1 may be controlled by negative feedback circuits induced early after infection.

# Structure
NLRX1 has a unique protein structure composed of 3 protein domains: an N-terminal effector domain containing a mitochondrion localization signal; a central NACHT domain; a C-terminal leucine-rich repeat (LRR) domain.
NPAS3
NPAS3 or Neuronal PAS domain protein 3 is a brain-enriched transcription factor belonging to the bHLH-PAS superfamily of transcription factors, the members of which carry out diverse functions, including circadian oscillations, neurogenesis, toxin metabolism, hypoxia, and tracheal development. NPAS3 contains basic helix-loop-helix structural motif and PAS domain, like the other proteins in the superfamily.

# Function
NPAS3 is also known as human accelerated region 21.  It may, therefore, have played a key role in differentiating humans from apes.
NPAS1 and NPAS3-deficient mice display behavioral abnormalities typical to the animal models of schizophrenia.
According to the same study, NPAS1 and NPAS3 disruption leads to reduced expression of reelin, which is also consistently found to be reduced in the brains of human patients with schizophrenia and psychotic bipolar disorder. Among the 49 genomic regions that undergone rapid changes in humans compared with their evolutionary ancestors, NPAS3 was found to be located in the region 21.

# Clinical significance
Disruption of NPAS3 was found in one family affected by schizophrenia and NPAS3 gene is thought to be associated with psychiatric illness and learning disability. In a genetic study of several hundred subjects conducted in 2008, interacting haplotypes at the NPAS3 locus were found to affect the risk of schizophrenia and bipolar disorder.
In a pharmacogenetical study, polymorphisms in NPAS3 gene were highly associated with response to iloperidone, a proposed atypical antipsychotic.
NPHP1
Nephrocystin-1 is a protein that in humans is encoded by the NPHP1 gene.

# Function
This gene encodes a protein with src homology domain 3 (SH3) patterns. Mutations in this gene cause familial juvenile nephronophthisis.

# Interactions
NPHP1 has been shown to interact with BCAR1, PTK2B, Filamin and INVS.
NPRL3
Nitrogen permease regulator-like 3 is a protein that in humans is encoded by the NPRL3 gene.

# Function
NPRL3 is a human protein of poorly understood function but has been associated with cancer.
The most prominent function ascribed to Nprl3 to date is as part of the GATOR1 complex (with NPRL2 and DEPDC5) that inhibits the mechanistic target of rapamycin (mTOR) kinase-complex-1 (mTORC1) on the surface of the lysosome (equivalent of degradative vacuole in yeast) via an effect on the Rag GTPase complex.  Additionally, Nprl3 has been shown to adjust cell metabolism via the TOR pathway, and this is important for development of the cardiovascular system in mammals. Without this effect, spontaneous cell apoptosis would occur. A similar function for Nprl3 has been identified in the female reproductive system of Drosophila during times of protein scarcity.

# Gene
In Homo sapiens, the NPRL3 gene is located at C16orf35. The gene is composed of 14 exons at 53 kbp in length. This gene is highly conserved in vertebrates which is upstream from the alpha globin gene cluster. Within the fifth intron of the gene there is a regulatory section of DNA HS-40 which regulates the expression of the alpha globin. This means that the gene C16orf35 is expressed in early erythrocytes accompanying hemoglobin production.

# Structure
The human nitrogen permease regulator-like 3 protein has 569 amino acids.

## Domains
There is a predicted N-terminal longin domain within the Nprl3 protein (amino acids 4-168). At the C terminus there are three consecutive winged helix turn helix (HTH) domains. These regions are predicted bind to another macromolecule, which could be DNA, RNA or protein.
NPTX2
Neuronal pentraxin-2 is a protein that in humans is encoded by the NPTX2 gene.

# Function
This gene encodes a member of the family of neuronal pentraxins, synaptic proteins that are related to C-reactive protein. This protein is involved in excitatory synapse formation. It also plays a role in clustering of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors at established synapses, resulting in non-apoptotic cell death of dopaminergic nerve cells.

# Clinical significance
Up-regulation of this gene in Parkinson disease (PD) tissues suggests that the protein may be involved in the pathology of PD.
NRIP1
Nuclear receptor-interacting protein 1 (NRIP1) also known as receptor-interacting protein 140 (RIP140) is a protein that in humans is encoded by the NRIP1 gene.

# Function
Nuclear receptor interacting protein 1 (NRIP1) is a nuclear protein that specifically interacts with the hormone-dependent activation domain AF2 of nuclear receptors. Also known as RIP140, this protein is a key regulator which modulates transcriptional activity of a variety of transcription factors, including the estrogen receptor.
RIP140 has an important role in regulating lipid and glucose metabolism, and regulates gene expression in metabolic tissues including heart, skeletal muscle, and liver.  A major role for RIP140 in adipose tissue is to block the expression of genes involved in energy dissipation and mitochondrial uncoupling, including uncoupling protein 1 and carnitine palmitoyltransferase 1b.
Estrogen-related receptor alpha (ERRa) can activate RIP140 during adipogenesis, by means of directly binding to an estrogen receptor element/ERR element and indirectly through Sp1 binding to the proximal promoter.
RIP140 suppresses the expression of mitochondrial proteins succinate dehydrogenase complex b and CoxVb and acts as a negative regulator of glucose uptake in mice.

# Knockout studies
Knockout mice that completely lack the RIP140 molecule are lean and stay lean, even on a rich diet.
Knockout mice (females) are also infertile because they fail to ovulate. Failure of ovulation in these mice is caused by lack of cumulus expansion and altered expression of various genes, including amphiregulin, in ovarian follicles.

# Clinical significance
RIP140 is part of the chain by which tumors can cause cachexia.
Levels of RIP140 expression in various tissues varies during aging in mice, suggesting changes in metabolic function. RIP140 is implicated in certain human disease processes. In morbid obesity, RIP140 levels are down-regulated in visceral adipose tissue. In breast cancer, RIP140 is involved in regulation of E2F1, an oncogene which discriminates between luminal and basal types of tumours.  RIP140 has an influence upon cancer phenotype and prognosis. In addition, RIP140 has a role in inflammation, since it acts as a coactivator for NFkappaB/RelA-dependent cytokine gene expression. Lack of RIP140 leads to an inhibition of proinflammatory pathways in macrophages.

# Interactions
NRIP1 has been shown to interact with:
- AHR,
- CTBP1
- CTBP2,
- DAX1,
- HDAC5,
- NR1B1,
- NR2B1,
- NR3A1,
- NR3C1,
- NR5A1, and
- YWHAQ.
NRXN1
Neurexin-1-alpha is a protein that in humans is encoded by the NRXN1 gene.
Neurexins are a family of proteins that function in the vertebrate nervous system as cell adhesion molecules and receptors. They are encoded by several unlinked genes of which two, NRXN1 and NRXN3, are among the largest known human genes. 
Three of the genes (NRXN1-3) utilize two alternate promoters and include numerous alternatively spliced exons to generate thousands of distinct mRNA transcripts and protein isoforms. The majority of transcripts are  produced from the upstream promoter and encode alpha-neurexin isoforms; a much smaller number of transcripts are produced from the downstream promoter and encode beta-neurexin isoforms. The alpha-neurexins contain epidermal growth factor-like (EGF-like) sequences and laminin G domains, and have been shown to interact with neurexophilins. The beta-neurexins lack EGF-like sequences and contain fewer laminin G domains than alpha-neurexins.

# Genomics
The gene is found in a single copy on the short arm of chromosome 2 (2p16.3). The gene is 1,112,187 bases in length, is located on the Crick (minus) strand and encodes a protein of 1,477 amino acids (molecular weight 161.883 kDa).
Mutations of this gene that interrupt its expression have been associated with schizophrenia, autism, and intellectual disability (NRXN1 mutations and brain disorders).

# Interactions
NRXN1 has been shown to interact with NLGN1.
NSUN2
NOP2/Sun domain family, member 2 is a protein that in humans is encoded by the NSUN2 gene. Alternatively spliced transcript variants encoding different isoforms have been noted for the gene.

# Function
The protein is a methyltransferase that catalyzes the methylation of cytosine to 5-methylcytosine (m5C) at position 34 of intron-containing tRNA (Leu)(CAA) precursors. This modification is necessary to stabilize the anticodon-codon pairing and correctly translate the mRNA.

# Clinical relevance
Mutations in this gene have been found associated to cases of Dubowitz-like syndrome.

# Model organisms
Model organisms have been used in the study of NSUN2 function. A conditional knockout mouse line, called Nsun2tm1a(EUCOMM)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 eight tests were carried out on mutant mice and fourteen significant abnormalities were observed. Homozygous mutants were subviable and had decreased body weights, length of long bones and decreased circulating glucose levels, numerous abnormal body composition, X-ray imaging, eye morphology and haematology parameters; males also had a decreased grip strength, a short upturned snout, and abnormal indirect calorimetry and plasma chemistry parameters. Males (but not females) were also infertile. 
In addition, heterozygote mutants displayed premature hair follicle exogen.
NTHL1
Endonuclease III-like protein 1 is an enzyme that in humans is encoded by the NTHL1 gene.
As reviewed by Li et al.,  NTHL1 is a bifunctional DNA glycosylase that has an associated beta-elimination activity.  NTHL1 is usually involved in removing oxidative pyrimidine lesions through base excision repair.  NTHL1 catalyses the first step in base excision repair.  It cleaves the N-glycosylic bond between the damaged base and its associated sugar residue and then cleaves the phosphodiester bond 3' to the AP site, leaving a 3'-unsaturated aldehyde after beta-elimination and a 5'-phosphate at the termini of the repair gap.
Low expression of NTHL1 is associated with initiation and development of astrocytoma.  Low expression of NTHL1 is also found in follicular thyroid tumors.
A germ line homozygous mutation in NTHL1 causes a cancer susceptibility syndrome similar to Lynch syndrome.
NUAK1
NUAK family SNF1-like kinase 1 also known as AMPK-related protein kinase 5 (ARK5) is an enzyme that in humans is encoded by the NUAK1 gene.

# Function

# Clinical significance
ARK5 is important in tumor malignancy and invasiveness.

# Research findings
ARK5 is often overexpressed in multiple myeloma cell lines.
ARK5 promotes tumor cell survival under regulation by Akt.
ARK5 increases MT1-MMP production. (MT1-MMP activates MMP-2 and MMP-9 which are involved in tumor metastasis.)

# As a drug target
ON123300 (a CDK4 inhibitor), also inhibits ARK5 and reduces proliferation of multiple myeloma and mantle cell lymphoma cell lines.

# Interactions
NUAK1 has been shown to interact with USP9X and Ubiquitin C.
NUBP2
Nucleotide-binding protein 2 (NBP 2) also known as cytosolic Fe-S cluster assembly factor NUBP2 is a protein that in humans is encoded by the NUBP2 gene.
NUBP2 is a member of the NUBP/MRP gene subfamily of ATP-binding proteins. There are two types in eukaryotes NUBP1 and NUBP2, and one novel human gene that define NBP nucleotide-binding proteins (NUBP/MRP-multidrug resistance-associated protein) in mammalian cells requires the maturation of cytosolic     iron-sulfur (Fe/S) proteins as Nubp1 is involved in the formation of extramitochondrial Fe/S proteins the cell division inhibitor MinD is homologous and involve two proteins components of the (FeS) protein assembly machinery closely similar cytosolic soluble P loop NTPase where Nar1 is required for assembly, identified Cfd1p in cytosolic and nuclear Fe/S protein biogenesis in yeast. Nubp proteins NTPase Nbp35p. MinD is homologous to members in MinD of E. coli, a relative of the ParA family.

# Morphology
Further information: Morphology (biology)
NBP35 bacterial plasmids F (the classical Escherichia coli sex factor) is found in all nuclear genes in vegetative and gametic flagella of the unicellular green algae  C. reinhardtii and nuclear Fe/S protein biogenesis required for cytosolic iron-sulfur protein assembly; MNP =MRP-like; MRP (Multiple Resistance and pH adaptation) MRP/NBP35-like P-loop NTPase similar to; and functions as minD_arch; cell division ATPase MinD, archaeal and homologue's of NUBP1. The NBP35 gene is conserved in archaea Bacteria, Metazoa, Fungi and other Eukaryotes and with considerable divergence from the yeast; Cfd1-Nbp35 Fe-S to man. In a scaffold complex protein to form large molecular assemblies that store Fe(III) and 4Fe-4S seen as secondary to defects inactivated to accomplish its functions as physiologically relevant form(s) Fe/S proteins Iron regulatory protein 1 (IRP1)  is regulated through prevents deficiencies and increased mutation rates that characterized a plant P loop NTPase with sequence similarity to Nbp35 homologue's of NUBP1.

# Interactions
NUBP2 has been shown to interact with...
- ACO1 Iron-responsive element-binding protein 1 (IRE-BP 1) (Iron regulatory protein 1) (IRP1)
- MAPK8IP3 C-jun-amino-terminal kinase-interacting protein 3 (JNK-interacting protein 3) (JIP-3)
- IGFALS Insulin-like growth factor-binding protein complex acid labile chain precursor (ALS)
- KIF11 Kinesin-like protein KIF11 (Kinesin-related motor protein Eg5)
- SEPP1 Selenoprotein P precursor (SeP)
- CA1 Carbonic anhydrase 1 (EC 4.2.1.1) (Carbonic anhydrase I) (Carbonate dehydratase I) (CA-I)
NUTF2
Nuclear transport factor 2 is a protein that in humans is encoded by the NUTF2 gene.

# Function
The protein encoded by this gene is a cytosolic factor that facilitates protein transport into the nucleus. It interacts with the nuclear pore complex glycoprotein p62. This encoded protein acts at a relative late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope. It is thought to be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import.

# Interactions
NUTF2 has been shown to interact with Nucleoporin 62{ and RAN.
Nisin
Nisin is a polycyclic peptide antibacterial with 34 amino acid residues used as a food preservative. It contains the uncommon amino acids lanthionine (Lan), methyllanthionine (MeLan), didehydroalanine (Dha) and didehydroaminobutyric acid (Dhb). These unusual amino acids are introduced by posttranslational modification of the precursor peptide. In these reactions a ribosomally synthesized 57-mer is converted to the final peptide. The unsaturated amino acids originate from serine and threonine, and the enzyme-catalysed addition of cysteine residues to the didehydro amino acids result in the multiple thioether bridges.
Structure of nisin
Nisin is produced by fermentation using the bacterium Lactococcus lactis. Commercially it is obtained from natural substrates including milk and is not chemically synthesized. It is used in processed cheese production to extend shelf life by suppressing gram-positive spoilage and pathogenic bacteria. There are many other applications of this preservative in food and beverage production. Due to its highly selective spectrum of activity it is also employed as a selective agent in microbiological media for the isolation of gram-negative bacteria, yeast and moulds. Subtilin and Epidermin are related to Nisin, all members of a class of molecules called lantibiotics.
As a food additive, nisin has E number E234.

# Further reading
- K. Fukase et al., Tetrahedron Lett. 1988, 29, 7, 795. (Total synthesis)
- G. W. Buchman et al., J. Biol. Chem. 1988, 263, 31, 16260. (Biosynthesis)
cs:Nisin
de:Nisin
nl:Nisine
Niter

# Overview
Niter (US) or nitre (UK) is the mineral form of potassium nitrate, KNO3, also known as saltpeter (US) or saltpetre (UK). Historically, the term "nitre"  cognate with "natrium", an old word for sodium  has been very vaguely defined, and it has been applied to a variety of other minerals and chemical compounds, including sodium nitrate (also "soda nitre" or "cubic nitre"), sodium carbonate and potassium carbonate. This article is about the mineral form of potassium nitrate, which is the usual modern meaning.
Niter is a colorless to white mineral crystallizing in the orthorhombic crystal system. It usually is found as massive encrustations and effervescent growths on cavern walls and ceilings where solutions containing alkali potassium and nitrate seep into the openings. It occasionally occurs as prismatic acicular crystal groups, and individual crystals commonly show twinning. It is most common in arid environments. It is a soft mineral equal to gypsum on the Mohs scale and has a low specific gravity of 2.1. It has refractive indices of n=1.332, n=1.504, and n=1.504. It readily dissolves in water.
Niter has been known since ancient times. The name is from Hebrew neter, for salt derived ashes.
In literature, Edgar Allan Poe invokes the supposed Saint of Nitre repeatedly in the short story "The Cask of Amontillado" (1846), in which the main character uses the nitre to his "advantages", as it slowly murders his enemy. Fortunato's health worsens, until Montresor takes his revenge in the form of immurement.
OPHN1
Oligophrenin-1 is a protein that in humans is encoded by the OPHN1 gene.

# Function
Oligophrenin 1 has 25 exons and encodes a Rho-GTPase-activating protein. The Rho protein are important mediators of intracellular signal transduction, which affects cell migration and cell morphogenesis.

# Clinical significance
Mutations in this gene are responsible for non-specific X-linked intellectual disability (previously called mental retardation).
OPHN1 syndrome is a rare disorder characterized by intellectual disability and changes in the part of the brain which controls movement and balance (cerebellum). The syndrome mainly affects males. It is characterized by low muscle tone (hypotonia), developmental and cognitive delay, early-onset seizures, abnormal behavior, characteristic facial features (long face, bulging forehead, under eye creases, deep set eyes, and large ears), crossed eyes (strabismus) and inability to coordinate movements.
  A small cerebellum and large ventricles can be seen on brain imaging (MRI). Treatment is supportive and includes physical, occupational and speech and language therapy.
OPHN1 syndrome is caused by mutations in the OPHN1 gene, which is located on the  X chromosome. Inheritance is X-linked. Some females who carry a mutation in the OPHN1 gene may have mild learning disabilities, mild cognitive impairment, strabismus, and subtle facial changes.
OR5L1
Olfactory receptor 5L1 is a protein that in humans is encoded by the OR5L1 gene.
Olfactory receptors interact with odorant molecules in the nose, to initiate a neuronal response that triggers the perception of a smell. The olfactory receptor proteins are members of a large family of G-protein-coupled receptors (GPCR) arising from single coding-exon genes. 
Olfactory receptors share a 7-transmembrane domain structure with many neurotransmitter and hormone receptors and are responsible for the recognition and G protein-mediated transduction of odorant signals. The olfactory receptor gene family is the largest in the genome. The nomenclature assigned to the olfactory receptor genes and proteins for this organism is independent of other organisms.
OR6A2
Olfactory receptor 6A2 is a protein that in humans is encoded by the OR6A2 gene.

# Function
Olfactory receptors interact with odorant molecules in the nose, to initiate a neuronal response that triggers the perception of a smell. The olfactory receptor proteins are members of a large family of G-protein-coupled receptors (GPCR) arising from single coding-exon genes. Olfactory receptors share a 7-transmembrane domain structure with many neurotransmitters and hormone receptors and are responsible for the recognition and G protein-mediated transduction of odorant signals. The olfactory receptor gene family is the largest in the genome. The nomenclature assigned to the olfactory receptor genes and proteins for this organism is independent of other organisms.

# Clinical significance
Variation in the OR6A2 gene has been identified as a likely cause of some people's strong dislike of coriander (also known as cilantro), often associating it with a combination of soap and vomit, while for others it is closer to the foul smelling odor emitted by stinkbugs. This is due to the presence of aldehyde chemicals, which are present in soap, various detergents, coriander, several species of stinkbugs and cinnamon.