Persius/hicric huggingface dataset:
NCAPH
Condensin complex subunit 2 also known as chromosome-associated protein H (CAP-H) or non-SMC condensin I complex subunit H (NCAPH) is a protein that in humans is encoded by the NCAPH gene. CAP-H is a subunit of condensin I, a large protein complex involved in chromosome condensation

# Function
CAP-H is a member of the barr protein family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. CAP-H is associated with mitotic chromosomes, except during the early phase of chromosome condensation. During interphase, the protein has a distinct punctate nucleolar localization.

# Model organisms
Model organisms have been used in the study of NCAPH function. A conditional knockout mouse line, called Ncaphtm1a(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 four tests were carried out on mutant mice and three significant abnormalities were observed. No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice and an increased susceptibility to bacterial infection was observed in male animals.
NCEH1
Neutral cholesterol ester hydrolase 1 (NCEH) also known as arylacetamide deacetylase-like 1 (AADACL1) or KIAA1363 is an enzyme that in humans is encoded by the NCEH1 gene.
NCEH is an enzyme located in the endoplasmic reticulum.  NCEH hydrolyzes 2-acetyl monoalkylglycerol ether, as part of an enzymatic pathway regulating the levels of platelet activating factor and lysophospholipids that may be involved in cancer development.

# Function
The enzymatic reaction catalyzed by NCEH is:
- 2-acetyl monoalkylglycerol ether  monoalkylglycerol ether
Monoalkylglycerol ethers (MAGEs) can then be converted to lysophospholipids alkyl-lysophosphatidic acid (alkyl-LPA) and alkyl-lysophosphatidylcholine (alkyl-LPC).
Controversial studies by one group also implicate the protein in the hydrolysis of cholesterol esters.  However, loss of the protein in mice selectively reduces 2-acetyl monoalkylglycerol ether activity throughout the body.

# Clinical significance
Evidence suggests a role for NCEH in cancer.  Cancer cell lines contain unusually high levels of the protein.  Reduction of the amount of NCEH1 in cancer cells reduces tumor migration and growth in mice and addition of alkyl-LPA restores these processes.
NCEH can break down organophosphates like the pesticide metabolite chlorpyrifos oxon.  Conversely, enzymatic activity can be inhibited by organophosphates.

# Structure
NCEH is a serine hydrolase that contains an N-terminal transmembrane domain, a central catalytic domain and a lipid-binding domain at its C-terminus.  The protein exists in three isoforms that result from differences in mRNA splicing.  Transcripts encode a protein for isoform a of 448, b of 440 and c of 275 amino acids long.
NDC80
Kinetochore protein NDC80 homolog is a protein that in humans is encoded by the NDC80 gene.

# Function
Ndc80 is one of the proteins of outer kinetochore. It forms a heterotetramer with proteins NUF2, SPC25, and SPC24. This protein complex has microtubule-binding  domains.
HEC is one of several proteins involved in spindle checkpoint signaling. This surveillance mechanism assures correct segregation of chromosomes during cell division by detecting unaligned chromosomes and causing prometaphase arrest until the proper bipolar attachment of chromosomes is achieved.

# Interactions
NDC80 has been shown to interact with MIS12, NEK2 and PSMC2.
NDEL1
Nuclear distribution protein nudE-like 1 is a protein that in humans is encoded by the NDEL1 gene.
This gene encodes a thiol-activated oligopeptidase that is phosphorylated in M phase of the cell cycle. Phosphorylation regulates the cell cycle-dependent distribution of this protein, with a fraction of the protein bound strongly to centrosomes in interphase and localized to mitotic spindles in early M phase. Overall, this protein plays a role in nervous system development. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

# Interactions
NDEL1 has been shown to interact with Cyclin-dependent kinase 5, YWHAE, PAFAH1B1 and DISC1.
NDRG1
Protein NDRG1 is a protein that in humans is encoded by the NDRG1 gene.
This gene is a member of the N-myc downregulated gene family which belongs to the alpha/beta hydrolase superfamily. The protein encoded by this gene is a cytoplasmic protein involved in stress responses, hormone responses, cell growth, and differentiation. Mutations in this gene have been reported to be causative the autosomal-recessive version of Charcot-Marie-Tooth disease known as CMT4D.
It has been reported that NDRG1 localizes to the endosomes and is a Rab4a effector involved in vesicular recycling.
As reviewed by Fang et al., NDRG1 is involved in embryogenesis and development, cell growth and differentiation, lipid biosynthesis and myelination, stress responses, immunity, DNA repair and cell adhesion among other functions.  NDRG1 is localised in the cytoplasm, nucleus and mitochondrion, at probabilities of 47.8%, 26.1% and 8.7%, respectively.  In response to DNA damage  NDRG1 translocates from the cytoplasm to the nucleus, where it may inhibit cell growth and promote DNA repair mechanisms.  It is suggested that NDRG1 acts as a stress response gene or potentially as a transcription factor.

# Functions in cancer and metastasis
As reviewed by Kovacevic et al., NDRG1 is a potent, iron-regulated growth and metastasis suppressor that was found to be negatively correlated with cancer progression in a number of tumors, including prostate, pancreatic, breast, and colon cancers.  NDRG1 has marked anti-oncogenic activity, being associated with decreased cell proliferation, migration, invasion, and angiogenesis.  The molecular functions of NDRG1 affect numerous signaling pathways that regulate cancer cell proliferation, invasion, angiogenesis, and migration.  Specifically, NDRG1 inhibits the oncogenic RAS, c-Src, phosphatidylinositol 3-kinase (PI3K), WNT, ROCK1/pMLC2, and nuclear factor-light chain enhancer of activated B cell (NF-B) pathways, while promoting expression of key tumor-suppressive molecules including phosphatase and tensin homolog, E-cadherin, and mothers against decapentaplegic homolog 4 (SMAD4).  Through its effects on E-cadherin and beta-catenin, which form the adherens junction and promote cell adhesion, NDRG1 also inhibits the epithelial to mesenchymal transition, an initial key step in metastasis.

# Functions in DNA repair and aging
In one of its functions at a molecular level, NDRG1 binds and stabilizes methyltransferases, chiefly O-6-methylguanine-DNA methyltransferase (MGMT), a DNA repair protein.  Thus, higher expression of NDRG1 can promote MGMT protein stability and activity.  Dominick et al. showed NDRG1 and MGMT protein expression was increased by 2-fold to 3-fold for each of three strains of mice (Snell, GHKRO, and PAPPA-KO) with increased longevity.  These authors strongly suggest a link between the increase in the MGMT DNA repair pathway and a delay in the aging process in these mouse strains.  This is consistent with the DNA damage theory of aging.
NEAT1
Nuclear Enriched Abundant Transcript 1 (NEAT1) is a  ~3.2 kb novel nuclear long non-coding RNA (RIKEN cDNA 2310043N10Rik). It is also known as Virus Inducible NonCoding RNA (VINC) or MEN epsilon RNA. It is transcribed from the multiple endocrine neoplasia locus.
Expression of NEAT1 is induced in mouse brains during infection by Japanese encephalitis virus and rabies virus. NEAT1 is constitutively expressed in a number of non-neuronal tissues and cell lines.
NEAT1 localizes to specific nuclear structures called paraspeckles. NEAT1 RNA interacts with a paraspeckle protein known as P54nrb or NONO and it is essential for paraspeckle formation. Some studies demonstrate that NEAT1 RNA is essential for the formation and maintenance of paraspeckles. Thus, this novel noncoding RNA appears to have an important structural role in the nuclear paraspeckles.
NEIL1
Endonuclease VIII-like 1 is an enzyme that in humans is encoded by the NEIL1 gene.
NEIL1 belongs to a class of DNA glycosylases homologous to the bacterial Fpg/Nei family. These glycosylases initiate the first step in base excision repair by cleaving bases damaged by reactive oxygen species (ROS) and introducing a DNA strand break via the associated lyase reaction.

# Targets
NEIL1 recognizes (targets) and removes certain ROS-damaged bases and then incises the abasic site via , elimination, leaving 3 and 5 phosphate ends. NEIL1 recognizes oxidized pyrimidines, formamidopyrimidines, thymine residues oxidized at the methyl group, and both stereoisomers of thymine glycol.  The best substrates for human NEIL1 appear to be the hydantoin lesions, guanidinohydantoin, and spiroiminodihydantoin that are further oxidation products of 8-oxoG.  NEIL1 is also capable of removing lesions from single-stranded DNA as well as from bubble and forked DNA structures.  Because the expression of NEIL1 is cell-cycle dependent, and because it acts on forked DNA structures and interacts with PCNA and FEN-1, it has been proposed that NEIL1 functions in replication associated DNA repair.

# Deficiency in cancer
NEIL1 is one of the DNA repair genes most frequently hypermethylated in head and neck squamous cell carcinoma (HNSCC).  When 160 human DNA repair genes were evaluated for aberrant methylation in HNSCC tumors, 62% of tumors were hypermethylated in the NEIL1 promoter region, causing NEIL1 messenger RNA and NEIL1 protein to be repressed.  When 8 DNA repair genes were evaluated in non-small cell lung cancer (NSCLC) tumors, 42% were hypermethylated in the NEIL1 promoter region.  This was the most frequent DNA repair deficiency found among the 8 DNA repair genes tested. NEIL1 was also one of six DNA repair genes found to be hypermethylated in their promoter regions in colorectal cancer.
While other DNA repair genes, such as MGMT and MLH1, are often evaluated for epigenetic repression in many types of cancer, epigenetic deficiency of NEIL1 is usually not evaluated, but might be of importance in such cancers as well.
DNA damage appears to be the primary underlying cause of cancer.  If DNA repair is deficient, DNA damage tends to accumulate. Such excess DNA damage may increase mutational errors during DNA replication due to error-prone translesion synthesis. Excess DNA damage may also increase epigenetic alterations due to errors during DNA repair. Such mutations and epigenetic alterations may give rise to cancer (see malignant neoplasms).
In colon cancer, germ line mutations in DNA repair genes cause only 25% of cases. However, methylation of the promoter region of DNA repair genes (including NEIL1), are frequently associated with colon cancers and may be an important causal factor for these cancers.
NELL1
Protein kinase C-binding protein NELL1 also known as NEL-like protein 1 (NELL1) or Nel-related protein 1 (NRP1) is a protein that in humans is encoded by the NELL1 gene.

# Function
This gene encodes a cytoplasmic protein that contains epidermal growth factor (EGF) -like repeats. The encoded heterotrimeric protein may be involved in cell growth regulation and differentiation. A similar protein in rodents is involved in craniosynostosis. An alternative splice variant has been described but its full-length sequence has not been determined.
Recent study by UCLA researchers shows that administering the protein NELL-1 intravenously stimulates significant bone formation through the regenerative ability of stem cells.
NFASC
Neurofascin is a protein that in humans is encoded by the NFASC gene.

# Function
Neurofascin is an L1 family immunoglobulin cell adhesion molecule (see L1CAM) involved in axon subcellular targeting and synapse formation during neural development.

# Clinical importance
A homozygous mutation causing loss of Nfasc155 causes severe congenital hypotonia, contractures of fingers and toes and no reaction to touch or pain.
NFKB1
Nuclear factor NF-kappa-B p105 subunit is a protein that in humans is encoded by the NFKB1 gene.
This gene encodes a 105 kD protein which can undergo cotranslational processing by the 26S proteasome to produce a 50 kD protein. The 105 kD protein is a Rel protein-specific transcription inhibitor and the 50 kD protein is a DNA binding subunit of the NF-kappaB (NF-B) protein complex. NF-B is a transcription factor that is activated by various intra- and extra-cellular stimuli such as cytokines, oxidant-free radicals, ultraviolet irradiation, and bacterial or viral products. Activated NF-B translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions; over 200 known genes are targets of NF-B in various cell types, under specific conditions. Inappropriate activation of NF-B has been associated with a number of inflammatory diseases while persistent inhibition of NF-B leads to inappropriate immune cell development or delayed cell growth.

# Model organisms
Model organisms have been used in the study of NFKB1 function. A conditional knockout mouse line, called Nfkb1tm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty five tests were carried out on mutant mice and six significant abnormalities were observed. Female homozygotes had a decreased respiratory quotient, increased circulating alkaline phosphatase level and increased leukocyte cell number. Male homozygotes showed an increased susceptibility to Salmonella infection, while homozygotes of both sex had decreased IgG1 and decreased regulatory T cell and NK cell numbers.

# Interactions
NFKB1 has been shown to interact with:
- BCL3,
- C22orf25,
- HDAC1,
- HMGA2
- IKK2,
- ITGB3BP,
- IB,
- LYL1,
- MAP3K7IP2,
- MAP3K8,
- MEN1,
- NFKB2,
- NFKBIE,
- NOTCH1,
- Nuclear receptor coactivator 1,
- RELA,
- RELB,
- STAT3,
- STAT6,  and
- TSC22D3.
NFKB2
Nuclear factor NF-kappa-B p100 subunit is a protein that in humans is encoded by the NFKB2 gene.

# Function
NF-B has been detected in numerous cell types that express cytokines, chemokines, growth factors, cell adhesion molecules, and some acute phase proteins in health and in various disease states. NF-B is activated by a wide variety of stimuli such as cytokines, oxidant-free radicals, inhaled particles, ultraviolet irradiation, and bacterial or viral products. Inappropriate activation of NF-kappa-B has been linked to inflammatory events associated with autoimmune arthritis, asthma, septic shock, lung fibrosis, glomerulonephritis, atherosclerosis, and AIDS. In contrast, complete and persistent inhibition of NF-kappa-B has been linked directly to apoptosis, inappropriate immune cell development, and delayed cell growth. For reviews, see Chen et al. (1999) and Baldwin (1996).

# Clinical significance
Mutation of the NFKB2 gene has been linked to Common variable immunodeficiency (CVID) as the cause of the disease. Other genes might also be responsible. The frequency of NFKB2 mutation in CVID population is yet to be established.
The protein NFKB2 can become mutated and lead to hereditary endocrine and immuneodeficiences. The mutation occurs at the C-terminus of NFKB2 and it causes common variable immunodeficienciency which in turn causes endocrine deficiency and immunodeficiencies. A NFKB2 mutation can cause things like adrenocorticotropic hormone deficiency and DAVID syndrome which is a pituitary hormone deficiency and CVID.
The mutations that occur within the C-terminus affect the serine 866 and 870. These serines are considered phosphorylation sites for NFKB2.  These mutations at the serines in the C-terminus lead to CVID in combination with other endocrine deficiencies. These endocrine deficiencies along with the mutation of NFKB2, lead scientists to believe that mutation of NFKB2 is a rare hereditary disease called DAVIDs disease.

# Interactions
NFKB2 has been shown to interact with:
- BCL3,
- BTRC,
- MAP3K8,
- NFKB1,
- NFKBIE,
- RELA,
- RELB,
- REL, and
- TSC22D3.
NIPA1
Non-imprinted in Prader-Willi/Angelman syndrome region protein 1 is a protein that in humans is encoded by the NIPA1 gene.
This gene encodes a potential transmembrane protein which functions either as a receptor or transporter molecule, possibly as a magnesium transporter. This protein is thought to play a role in nervous system development and maintenance. Alternative splice variants have been described, but their biological nature has not been determined. Mutations in this gene have been associated with the human genetic disease autosomal dominant spastic paraplegia 6.

# Model organisms
Model organisms have been used in the study of NIPA1 function. A conditional knockout mouse line, called Nipa1tm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists  at the Wellcome Trust Sanger Institute.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty four tests were carried out on mutant mice but no significant abnormalities were observed.
NIPBL
Nipped-B-like protein (Nipbl), also known as Scc2 or delangin is a protein that in humans is encoded by the NIPBL gene. Nipbl is required for the association of cohesin with DNA and is the major subunit of the cohesin loading complex. Heterozygous mutations in NIPBL account for an estimated 60% of case of Cornelia de Lange Syndrome.

# Function
Nipbl is a large hook-shaped protein containing HEAT repeats. Nipbl forms a complex with Mau4 known as the cohesin loading complex or Kollerin. Cohesin is a ring-shaped protein complex responsible for sister chromatid cohesion. Cohesin is also thought to mediate enhancer-promoter interactions and generate Topologically associating domain. As well as mediating cohesion and regulating DNA architecture the cohesin complex is required for DNA repair by homologous recombination. Given that Nipbl is required for cohesin's association with DNA it is thought that Nipbl is also required for all of these processes. Consistently, inactivation of Nipbl results in the loss topologically associating domains and cohesion. Nipbl/Scc2 binds dynamically to chromatin principally through an association with cohesin.  Nipbls movement within chromatin is consistent with a mechanism involving hopping between chromosomal cohesin rings.
A cohesin-independent function in the regulation of gene expression has also been demonstrated for Nipbl.

# Clinical significance
Mutations in this gene result in Cornelia de Lange syndrome (CdLS), a disorder characterized by dysmorphic facial features, growth delay, limb reduction defects, and mental retardation. As these mutations are usually heterozygous, CdLS is caused by a reduction in the abundance of Nipbl not a complete loss. Experiments on cells from patients and mice indicate that the reduction is by less than half. It is not known why a reduction in Nipbl expression results in CdLS.
NISCH
Nischarin is a protein that in humans is encoded by the NISCH gene.

# Function
This gene encodes a nonadrenergic imidazoline-1 receptor protein that localizes to the cytosol and anchors to the inner layer of the plasma membrane. The orthologous mouse protein has been shown to influence cytoskeletal organization and cell migration by binding to alpha-5-beta-1 integrin. In humans, this protein has been shown to bind to the adapter insulin receptor substrate 4 (IRS4) to mediate translocation of alpha-5 integrin from the cell membrane to endosomes. In human cardiac tissue, this gene was found to affect cell growth and death while in neural tissue it affected neuronal growth and differentiation.

# Clinical significance
Expression of this protein was reduced in human breast cancers while its overexpression reduced tumor growth and metastasis; possibly by limiting the expression of alpha-5 integrin.

# Interactions
NISCH has been shown to interact with IRS4.
NLRC4
NLR family CARD domain-containing protein 4 is a protein that in humans is encoded by the NLRC4 gene.

# Structure
The NLRC4 protein is highly conserved across mammalian species. It bears homology to the C. elegans Ced4 protein. It contains an n-terminal CARD domain, a central nucleotide binding/NACHT domain, and a c-terminal leucine rich repeat (LRR) domain. It belongs to a family of NLR proteins that includes the transcriptional co-activator CIITA and the canonical inflammasome protein NLRP3. A truncated murine NLRC4 was the first member of this family whose crystal structure was solved.

# Function
NLRC4 is best associated with triggering formation of the inflammasome. Unlike NLRP3, certain inflammasome-dependent functions of NLRC4 may be carried out independently of the inflammasome scaffold ASC.  Human Ced4 homologs include APAF1, NOD1 (CARD4), and NOD2 (CARD15). These proteins have at least 1 N-terminal CARD domain followed by a centrally located  nucleotide-binding domain (NBD or NACHT) and a C-terminal regulatory domain, found only in mammals, that contains either WD40 repeats or leucine-rich repeats (LRRs). CARD12 is a member of the Ced4 family and can induce apoptosis.

# Interactions
NLRC4 has been shown to interact with NAIP (there is one human NAIP but mice express at least 4 distinct NAIP proteins). The NAIP/NLRC4 interaction may determine the ligand specificity. NLRC4-dependent inflammasome activity activates CASP1. Under certain circumstances, NLRC4 and NLRP3 may occupy the same inflammasome complex.

# Clinical significance
Humans bearing activating mutations in NLRC4 can develop an autoinflammatory syndrome characterized by acute fever, hepatitis, very high serum ferritin, and other features suggestive of Macrophage Activation Syndrome (MAS). Some patients also developed a potentially life-threatening enterocolitis that abated during early childhood. In these patients, chronic and extraordinary elevation of serum IL-18 is found, in distinction from patients with NLRP3 mutations who develop Cryopyrin Associated Periodic Syndromes. A large Japanese family had much milder disease associated with cold-induced urticaria that was caused by a dominantly inherited NLRC4 mutation.
NLRC5
NLRC5, short for NOD-like receptor family CARD domain containing 5, is an intracellular protein that plays a role in the immune system.  NLRC5 is a pattern recognition receptor implicated in innate immunity to viruses potentially by regulating interferon activity.
Recently, NLRC5 has been suggested to play a positive role in the regulation of Major Histocompatibility Class I (MHCI) molecule expression. This aspect of NLRC5 function was further investigated with the help of Nlrc5-deficient mice, which showed reduced MHCI expression in lymphocytes (particularly T, NK and NKT lymphocytes). In lymphocytes, NLRC5 localizes to the nucleus and drives MHCI gene expression by occupying H-2D and H-2K gene promoters.
In humans, the NLRC5 protein is encoded by the NLRC5 gene. It has also been called NOD27, NOD4, and CLR16.1.