Persius/hicric huggingface dataset:
FABP7
Fatty acid binding protein 7, brain (FABP7; also brain lipid binding protein, BLBP), is a human gene.

# Function
The protein encoded by this gene is a brain fatty acid binding protein. Fatty acid binding proteins (FABPs) are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs are thought to play roles in fatty acid uptake, transport, and metabolism.
FABP7 is expressed, during development, in radial glia by the activation of Notch receptors. Reelin was shown to induce FABP7 expression in neural progenitor cells via Notch-1 activation.
According to one study, FABP7 binds DHA with the highest affinity among all of the FABPs.

# Role in pathology
FABP7 maps onto human chromosome 6q22.31, a schizophrenia linkage region corroborated by a meta-analysis.
As of 2008, two studies have been conducted into FABP7 as a possible risk gene for schizophrenia, with one, that tested for only one SNP, showing negative and another, with seven SNPs, a positive result. The effect of the gene in the latter study was stronger in males. This study also linked FABP7 variation to weak prepulse inhibition in mice; deficit in PPI is an endophenotypic trait observed in schizophrenia patients and their relatives.
FADS1
Fatty acid desaturase 1 is an enzyme that in humans is encoded by the FADS1 gene.

# Function
The protein encoded by the FADS1 gene is a member of the fatty acid desaturase (FADS) gene family and desaturates omega-3 and omega-6 polyunsaturated fatty acids at the delta-5 position, catalyzing the final step in the formation of eicosapentaenoic acid (EPA) and Arachidonic acid. Desaturase enzymes (such as those encoded by FADS1) regulate unsaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl chain. FADS family members are considered fusion products composed of an N-terminal cytochrome b5-like domain and a C-terminal multiple membrane-spanning desaturase portion, both of which are characterized by conserved histidine motifs. This gene is clustered with family members FADS1 and FADS2 at 11q12-q13.1; this cluster is thought to have arisen evolutionarily from gene duplication based on its similar exon/intron organization.

# Clinical significance
Single nucleotide polymorphisms (SNPs) of FADS1 and FADS2 may affect long-chain polyunsaturated fatty acids (LC-PUFA) metabolism and have a potential role in the development of atopic diseases.
FADS2
This article is about the gene, for main associated enzyme see D6D.
Fatty acid desaturase 2 (FADS2) is encoded by the FADS2 gene, the associated enzyme is sometimes known as FADS2 as well.  Its main associated enzyme is Delta 6 desaturase (D6D) however the human enzyme been shown to also catalyze some delta-8 and delta-4 desaturases in spite of naming conventions.

# Function
Fatty acid desaturase 2 is a member of the fatty acid desaturase (FADS) gene family. Desaturase enzymes cause desaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl chain. FADS family members are considered fusion products composed of an N-terminal cytochrome b5-like domain and a C-terminal multiple membrane-spanning desaturase portion, both of which are characterized by conserved histidine motifs. This gene is clustered with family members FADS1 and FADS2 at 11q12-q13.1; this cluster is thought to have arisen evolutionarily from gene duplication based on its similar exon/intron organization.

# Clinical significance
It was reported the FADS2 interacts with breastfeeding such that breast-fed children with the "C" version of the gene appear about 7 intelligence quotient (IQ) points higher than those with the less common "G" version (less than this when adjusted for maternal IQ).
An attempt to replicate this study in 5934 8 year old children failed: No relationship of the common C allele to negative effects of formula feeding was apparent, and contra to the original report, the rare GG homozygote children performed worse when formula fed than other children on formula milk. A study of over 700 families recently found no evidence for either main or moderating effects of the original SNP (rs174575), nor of two additional FADS2 polymorphisms (rs1535 and rs174583), nor any effect of maternal FADS2 status on offspring IQ.
FAHD1
Fumarylacetoacetate hydrolase domain-containing protein 1, also known as FLJ36880 protein, is an enzyme that in humans is encoded by the FAHD1 gene on chromosome 16.

# Structure
The FAHD1 gene encodes for a 24-kDa protein that is localized to the mitochondrion and belongs to the fumarylacetoacetate hydrolase family of proteins. The structure of FAHD1 has been resolved using X-ray crystallography at 2.2-A resolution. The overall structure is similar to the C-terminal domain of the bifunctional enzyme HpcE from Escherichia coli C, fumarylacetoacetate hydrolase from Mus musculus and to YcgM (Apc5008) from E. coli 1262. A number of conserved amino acids including Asp-102 and Arg-106 of FAHD1 appear to be important for its catalytic activity.

# Function
The FAHD1 protein has been shown to function as an oxaloacetate decarboxylase in eukaryotes. The FAHD1 protein probably also functions as an acylpyruvase, having been shown to catalyze the hydrolysis of acetylpyruvate and fumarylpyruvate in in vitro experiments.  Mg(2+) was required for maximal enzyme activity.
FANCB
Fanconi anemia group B protein is a protein that in humans is encoded by the FANCB gene.

# Function
The Fanconi anemia complementation group (FANC) currently includes FANCA, FANCB, FANCC, FANCD1 (also called BRCA2), FANCD2, FANCE, FANCF, FANCG, and FANCL. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation group B. Alternative splicing results in two transcript variants encoding the same protein.

# Gene
FANCB is the only gene known to cause X-linked Fanconi Anemia. In female carriers of FANCB mutations (one wild-type FANCB allele and one mutant FANCB allele) there is strong selection through X-inactivation for expression of only the wild-type allele. In contrast, males have only one FANCB allele. Only male patients with Fanconi anemia have ever been linked to FANCB mutations, and they make up about 4% of cases.

# Protein
The FANCB gene product is FANCB protein. FANCB is a component of a "core complex" of nine Fanconi Anemia proteins: FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FAAP100 and FAAP20. The core complex localises to DNA damage sites during DNA replication where it catalyzes transfer of ubiquitin to FANCD2 and FANCI. In particular, this reaction is necessary for the repair of DNA interstrand crosslinks, such as those formed by chemotherapy drugs cisplatin, mitomycin c and melphalan.
Within the Fanconi anemia core complex, FANCB has an obligate interaction with FAAP100 and FANCL, to form a catalytic E3 RING ligase enzyme. FANCB creates a dimer interface within this subcomplex that is required for simultaneous ubiquitination of FANCD2 and FANCI. Electron microscopy imaging of the FANCB-FANCL-FAAP100 complex revealed a symmetry that is centred on FANCB, and biochemical investigation confirmed that the entire complex is a dimer containing two of each subunit. Further imaging reveals the overall architecture of the Fanconi Anemia core complex centres on FANCB protein.

# Meiosis
FANCB mutant mice are infertile and exhibit primordial germ cell defects during embryogenesis.  The germ cells and testicular size are severely compromised in FANCB mutant mice.  FANCB protein is essential for spermatogenesis and  likely has a role in the activation of the Fanconi anemia DNA repair pathway during meiosis.
FANCF
Fanconi anemia group F protein is a protein that in humans is encoded by the FANCF gene.

# Interactions
FANCF has been shown to interact with Fanconi anemia, complementation group C, FANCG, FANCA and FANCE.

# Function
FANCF is an adaptor protein that plays a key role in the proper assembly of the FA core complex. The FA core complex is composed of eight proteins (FANCA, -B, -C, -E, -F, -G, -L and -M).  FANCF stabilizes the interaction between the FANCC/FANCE subcomplex and the FANCA/FANCG subcomplex and locks the whole FA core complex in a conformation that is essential to perform its function in DNA repair.
The FA core complex is a nuclear core complex that is essential for the monoubiquitination of FANCD2 and this modified form of FANCD2 colocalizes with BRCA1, RAD51 and PCNA in foci that also contain other DNA repair proteins.  All these proteins function together to facilitate DNA interstrand cross-link repair.  They also function in other DNA damage response repair processes including recovering and stabilizing stalled replication forks.  FoxF1 protein also interacts with the FA protein core and induces its binding to chromatin to promote DNA repair.

# Cancer
DNA damage appears to be the primary underlying cause of cancer, and deficiencies in expression of DNA repair genes appear to underlie many forms of cancer.  If DNA repair is deficient, DNA damage tends to accumulate. Such excess DNA damage may increase mutations 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.
Reductions in expression of DNA repair genes (usually caused by epigenetic alterations) are very common in cancers, and are most often much more frequent than mutational defects in DNA repair genes in cancers. (Also see Frequencies of epimutations in DNA repair genes.)
Methylation of the promoter region of the FANCF gene causes reduced expression of FANCF protein.
The frequencies of FANCF promoter methylation in several different cancers is indicated in the table.
In invasive breast cancers, microRNA-210 (miR-210) was increased, along with decreased expression of FANCF, where FANCF was one of the likely targets of miR-210.
Although mutations in FANCF are ordinarily not observed in human tumors, an FANCF-deficient mouse model was prone to ovarian cancers.
FANCF appears to be one of about 26 DNA repair genes that are epigenetically repressed in various cancers (see Cancer epigenetics).

# Infertility
The gonads of FANCF mutant mice function abnormally, having compromised follicle development and spermatogenesis as has been observed in other Fanconi anemia mouse models and in Fanconi anemia patients.  Histological examination of the testes from FANCF-deficient mice showed that the seminiferous tubules were devoid of germ cells.  At 14 weeks of age, FANCF-deficient female mice were almost or completely devoid of primordial follicles.  It was concluded that FANCF-deficient mice display a rapid depletion of primordial follicles at a young age resulting in advanced ovarian aging.
FANCG
Fanconi anemia group G protein is a protein that in humans is encoded by the FANCG gene.

# Function
FANCG, involved in  Fanconi anemia, confers resistance to both hygromycin B and mitomycin C. FANCG contains a 5-prime GC-rich untranslated region characteristic of housekeeping genes. The putative 622-amino acid protein has a leucine-zipper motif at its N-terminus.  Fanconi anemia is an autosomal recessive disorder with diverse clinical symptoms, including developmental anomalies, bone marrow failure, and early occurrence of malignancies. A minimum of 8 FA genes have been identified. The FANCG gene is responsible for complementation group G.
The clinical phenotype of all Fanconi anemia (FA) complementation groups is similar.  This phenotype is characterized by progressive bone marrow failure, cancer proneness and typical birth defects.  The main cellular phenotype is hypersensitivity to DNA damage, particularly inter-strand DNA crosslinks.  The FA proteins interact through a multiprotein pathway.  DNA interstrand crosslinks are highly deleterious damages that are repaired by homologous recombination involving coordination of FA proteins and breast cancer susceptibility gene 1 (BRCA1), but the exact biochemical roles of these proteins is currently unclear.
A nuclear complex containing FANCG (as well as FANCA, FANCB, FANCC, FANCE, FANCF, FANCL and FANCM) is essential for the activation of the FANCD2 protein to the mono-ubiquitinated isoform.  In normal, non-mutant, cells FANCD2 is mono-ubiquinated in response to DNA damage.  Activated FANCD2 protein co-localizes with BRCA1 (breast cancer susceptibility protein) at ionizing radiation-induced foci and in synaptonemal complexes of meiotic chromosomes (see Figure: Recombinational repair of double strand damage).

# Meiosis
Activated FANCD2 protein may function prior to the initiation of meiotic recombination, perhaps to prepare chromosomes for synapsis, or to regulate subsequent recombination events.
Male and female FANCG mutant mice have defective gametogenesis, hypogonadism and impaired fertility, consistent with the phenotype of FA patients.  In the non-mutant mouse, FANCG protein is expressed in spermatogonia, preleptotene spermatocytes and spermatocytes in the leptotene, zygotene and early pachytene stages of meiosis.

# Aging
Loss of FANCG causes neural progenitor apoptosis during forebrain development, likely related to defective DNA repair. (Sii-Felice et al., 2008).  This effect persists in adulthood leading to depletion of the neural stem cell pool with aging.  The FA phenotype can be interpreted as a premature aging of stem cells, DNA damages being the driving force of aging. (Also see DNA damage theory of aging).

# Interactions
FANCG has been shown to interact with FANCF,
FANCA, FANCE and BRCA2.
FANCL
E3 ubiquitin-protein ligase FANCL is an enzyme that in humans is encoded by the FANCL gene.

# Function
The clinical phenotype of mutational defects in all Fanconi anemia (FA) complementation groups is similar.  This phenotype is characterized by progressive bone marrow failure, cancer proneness and typical birth defects.  The main cellular phenotype is hypersensitivity to DNA damage, particularly inter-strand DNA crosslinks.  The FA proteins interact through a multi-protein pathway.  DNA interstrand crosslinks are highly deleterious damages that are repaired by homologous recombination involving coordination of FA proteins and breast cancer susceptibility gene 1 (BRCA1).
The Fanconi Anemia (FA) DNA repair pathway is essential for the recognition and repair of DNA interstrand crosslinks (ICL).  A critical step in the pathway is the monoubiquitination of FANCD2 by the RING E3 ligase FANCL. FANCL comprises 3 domains, a RING domain that interacts with E2 conjugating enzymes, a central domain required for substrate interaction, and an N-terminal E2-like fold (ELF) domain that interacts with FANCB. The ELF domain of FANCL is also required to mediate a non-covalent interaction
between FANCL and ubiquitin. The ELF domain is required to promote efficient DNA damage-induced FANCD2 monoubiquitination in vertebrate cells, suggesting an important function of FANCB and ubiquitin binding by FANCL in vivo.
A nuclear complex containing FANCL (as well as FANCA, FANCB, FANCC, FANCE, FANCF, FANCG and FANCM) is essential for the activation of the FANCD2 protein to the mono-ubiquitinated isoform.  In normal, non-mutant, cells FANCD2 is mono-ubiquinated in response to DNA damage.  Activated FANCD2 protein co-localizes with BRCA1 (breast cancer susceptibility protein) at ionizing radiation-induced foci and in synaptonemal complexes of meiotic chromosomes (see Figure: Recombinational repair of double strand damage).
FANCM
Fanconi anemia, complementation group M, also known as FANCM is a human gene.

# Function
The protein encoded by this gene, FANCM displays DNA binding against fork structures and an ATPase activity associated with DNA branch migration. It is believed that FANCM in conjunction with other Fanconi anemia- proteins repair DNA at stalled replication forks, and stalled transcription structures called R-loops.
The structure of the C-terminus of FANCM (amino acids 1799-2048), bound to a partner protein FAAP24, reveals how the protein complex recognises branched DNA. A structure of amino acids 675-790 of FANCM reveal how the protein binds duplex DNA through a remodeling of the MHF1:MHF2 histone-like protein complex.

# Disease linkage
Homozygous mutations in the FANCM gene are associated with Fanconi anemia, although several individuals with FANCM deficiency do not appear to have the disorder. A founder mutation in the Scandinavian population is also associated with a higher than average frequency of triple negative breast cancer in heterozygous carriers. FANCM carriers also have elevated levels of Ovarian cancer and other solid tumours

# Meiosis
Recombination during meiosis is often initiated by a DNA double-strand break (DSB). During recombination, sections of DNA at the 5' ends of the break are cut away in a process called resection. In the strand invasion step that follows, an overhanging 3' end of the broken DNA molecule then "invades" the DNA of an homologous chromosome that is not broken forming a displacement loop (D-loop). After strand invasion, the further sequence of events may follow either of two main pathways leading to a crossover (CO) or a non-crossover (NCO) recombinant (see Genetic recombination and Homologous recombination).  The pathway leading to a NCO is referred to as synthesis dependent strand annealing (SDSA).
In the plant Arabidopsis thaliana FANCM helicase antagonizes the formation of CO recombinants during meiosis, thus favoring NCO recombinants.  The FANCM helicase is required for genome stability in humans and yeast, and is a major factor limiting meiotic CO formation in A. thaliana.  A pathway involving another helicase, RECQ4A/B, also acts independently of FANCM to reduce CO recombination.  These two pathways likely act by unwinding different joint molecule substrates (e.g. nascent versus extended D-loops; see Figure).
Only about 4% of DSBs in A. thaliana are repaired by CO recombination; the remaining 96% are likely repaired mainly by NCO recombination.  Sequela-Arnaud et al. suggested that CO numbers are restricted because of the long-term costs of CO recombination, that is, the breaking up of favorable genetic combinations of alleles built up by past natural selection.
In the fission yeast Schizosaccharomyces pombe, FANCM helicase also directs NCO recombination during meiosis.
FARP2
FERM, RhoGEF and pleckstrin domain-containing protein 2 is a protein that in humans is encoded by the FARP2 gene.

# Model organisms
Model organisms have been used in the study of FARP2 function. A conditional knockout mouse line, called Farp2tm1a(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 four tests were carried out on mutant mice and two significant abnormalities were observed. Homozygous mutant animals had a thickened cerebral cortex and displayed abnormal hair shedding.

# Interactions
FARP2 has been shown to interact with PDZK1.
FATE1
Fetal and Adult Testis-Expressed 1, encoded by the FATE1 gene in humans, is a protein identified as a cancer-testis antigen (CTA) in hepatocellular carcinomas and gastric and colon cancers. It is testis-specific in the fetus (aged 6  11 weeks). In adults, it is expressed predominantly in the testis and adrenal glands, with some expression in the lungs, heart, kidneys and throughout the brain.
FATE1 is member of the Miff protein family, with its C-terminal domain, consisting of a transmembrane domain with a coiled-coil domain, showing high similarity to the mitochondrial fission factor (MFF) protein which is involved in mitochondrial and peroxisomal fission.

# Gene location
FATE1 gene in humans is located on the long arm of the X chromosome at region 28, from base pair 150,884,502 to base pair 150,891,617.

# Mechanism
It has been hypothesized that FATE1 uses its C-terminal transmembrane domain to attach to endoplasmic reticulum (ER) membrane and with its C-terminal coiled-coil domain it interacts with mitochondria.
FATE1 is localized in mitochondria-associated ER membranes (MAM) and modulates ER-mitochondria distance to regulate Ca2+- and drug dependent apoptosis in cancer cells.
FATE1 expression leads to reduction of Ca2+ uptake by mitochondria and therefore decrease in fragmentation of mitochondria, associated with mitochondrial Ca2+ uptake, consequently providing protection against cell death.

# Relation to cancer
FATE1 is detectable in all cell lines derived from tumors, but is low or undetectable in telomere immortalized, non-tumorigenic fibroblasts and lung epithelial cells. FATE1 is suggested to be essential for survival of tumor cells as depletion of FATE1 results in viability reduction in melanoma, breast, prostate and sarcoma settings.
Upregulation of FATE1 by a transcription factor steroidogenic factor-1 (SF-1), involved in adrenal and gonadal development as well as in adrenocortical carcinoma, increases ER-mitochondria distance and is utilized by cancer cell to functionally uncouple ER and mitochondria.
Silencing FATE1 gene sensitizes non-small-cell lung cancer cell lines to paclitaxel, a chemotherapeutic drug against many different types of cancers.
Elevated level of FATE1 is found to be associated with higher mortality rate in colorectal cancers, but in non-small-cell lung cancers, elevation of FATE1 alone did not decrease chance of survival, but decreased if RNF183 expression is also increased.
FBLN1
FBLN1 is the gene encoding fibulin-1, an extracellular matrix and plasma protein.

# Function
Fibulin-1 is a secreted glycoprotein that is found in association with extracellular matrix structures including fibronectin-containing fibers, elastin-containing fibers and basement membranes. Fibulin-1 binds to a number of extracellular matrix constituents including fibronectin, nidogen-1, and the proteoglycan, versican. Fibulin-1 is also a blood protein capable of binding to fibrinogen.

# Structure
Fibulin-1 has modular domain structure and includes a series of nine epidermal growth factor-like modules followed by a fibulin-type module, a module found in all members of the fibulin gene family.
The human fibulin-1 gene, FBLN1, encodes four splice variants designated fibulin-1A, B, C and D, which differ in their carboxy terminal regions. In mouse, chicken and the nematode, C. elegans, only two fibulin-1 variants are produced, fibulin-1C and fibulin-1D.

# Interactions
FBLN1 has been shown to interact with:
- NOV/CCN3,
- amyloid precursor protein,
- entactin,
- fibrinogen, and
- fibronectin.
FBLN2
Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.
This gene encodes an extracellular matrix protein, which belongs to the fibulin family. This protein binds various extracellular ligands and calcium. It may play a role during organ development, in particular, during the differentiation of heart, skeletal and neuronal structures. Alternatively spliced transcript variants encoding different isoforms have been identified.

# Interactions
FBLN2 has been shown to interact with Laminin, alpha 1, Laminin, alpha 5 and Perlecan.