source stringlengths 32 209 | text stringlengths 18 1.5k |
|---|---|
https://en.wikipedia.org/wiki/GSTA2 | Glutathione S-transferase A2 is an enzyme that in humans is encoded by the GSTA2 gene.
Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding these enzymes are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of some drugs. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase belonging to the alpha class. The alpha class genes, located in a cluster mapped to chromosome 6, are the most abundantly expressed glutathione S-transferases in liver. In addition to metabolizing bilirubin and certain anti-cancer drugs in the liver, the alpha class of these enzymes exhibit glutathione peroxidase activity thereby protecting the cells from reactive oxygen species and the products of peroxidation.
References
Further reading |
https://en.wikipedia.org/wiki/HOXA5 | Homeobox protein Hox-A5 is a protein that in humans is encoded by the HOXA5 gene.
Function
In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation. Methylation of this gene may result in the loss of its expression and, since the encoded protein upregulates the tumor suppressor p53, this protein may play an important role in tumorigenesis.
HoxA5 is controlled, at least in part, by DNA methylation. HoxA5 has been shown to upregulate the tumor suppressor p53 and AKT1 by downregulation of PTEN. Suppression of HoxA5 has been shown to attenuate hemangioma growth. HoxA5 has far-reaching effects on gene expression, causing ~300 genes to become upregulated upon its induction in breast cancer cell lines. HoxA5 protein transduction domain overexpression prevents inflammation shown by inhibition of TNFα-inducible monocyte binding to HUVECs.
Comparison of the HoxA5 promoter methylation profile across cell types from the least differentiated (human embryonic stem cells) to the most endothelial-like (human umbilical vein endothelial cells, or HUVECs) shows that the HoxA5 promoter is normally heavily methylated in non |
https://en.wikipedia.org/wiki/HOXA11 | Homeobox protein Hox-A11 is a protein that in humans is encoded by the HOXA11 gene.
Function
In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation. This gene is involved in the regulation of uterine development and is required for female fertility. Mutations in this gene can cause radioulnar synostosis with amegakaryocytic thrombocytopenia.
See also
Homeobox
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/HES1 | Transcription factor HES1 (hairy and enhancer of split-1) is a protein that is encoded by the Hes1 gene, and is the mammalian homolog of the hairy gene in Drosophila. HES1 is one of the seven members of the Hes gene family (HES1-7). Hes genes code nuclear proteins that suppress transcription.
This protein belongs to the basic helix-loop-helix (bHLH) family of transcription factors. It is a transcriptional repressor of genes that require a bHLH protein for their transcription. The protein has a particular type of basic domain that contains a helix interrupting protein that binds to the N-box promoter region rather than the canonical enhancer box (E-box). As a member of the bHLH family, it is a transcriptional repressor that influences cell proliferation and differentiation in embryogenesis. HES1 regulates its own expression via a negative feedback loop, and oscillates with approximately 2-hour periodicity.
Structure
There are three conserved domains in Hes genes that impart transcriptional functions: the bHLH domain, the Orange domain, and the WRPW motif. Hes genes differ from other bHLH factors in that they have a proline residue in the middle of the basic DNA binding region. This proline has been proposed to give Hes proteins unique DNA binding capacity. While most bHLH factors bind to the E-box consensus sequence (CANNTG) that is present in the promoter region of target genes, Hes factors bind more preferentially to the Class C site or N box (CACNAG). The Orange domain |
https://en.wikipedia.org/wiki/STAM2 | Signal transducing adapter molecule 2 is a protein that in humans is encoded by the STAM2 gene.
Function
The protein encoded by this gene is closely related to STAM, an adaptor protein involved in the downstream signaling of cytokine receptors, both of which contain a SH3 domain and the immunoreceptor tyrosine-based activation motif (ITAM). Similar to STAM, this protein acts downstream of JAK kinases, and is phosphorylated in response to cytokine stimulation. This protein and STAM thus are thought to exhibit compensatory effects on the signaling pathway downstream of JAK kinases upon cytokine stimulation.
Interactions
STAM2 has been shown to interact with HGS, Janus kinase 1 and USP8.
References
Further reading
External links |
https://en.wikipedia.org/wiki/RTN3 | Reticulon-3 is a protein that in humans is encoded by the RTN3 gene.
The reticulons are a group of highly conserved genes with preferential expression in neuroendocrine tissues (see, e.g., RTN1; MIM 600865).[supplied by OMIM]
References
Further reading
External links |
https://en.wikipedia.org/wiki/KLF2 | Krüppel-like Factor 2 (KLF2), also known as lung Krüppel-like Factor (LKLF), is a protein that in humans is encoded by the KLF2 gene on chromosome 19. It is in the Krüppel-like factor family of zinc finger transcription factors, and it has been implicated in a variety of biochemical processes in the human body, including lung development, embryonic erythropoiesis, epithelial integrity, T-cell viability, and adipogenesis.
Discovery
Erythroid Krüppel-like Factor (EKLF or KLF1) was the first Krüppel-like Factor discovered. It is vital for embryonic erythropoiesis in promoting the switch from fetal hemoglobin (Hemoglobin F) to adult hemoglobin (Hemoglobin A) gene expression by binding to highly conserved CACCC domains. EKLF ablation in mouse embryos produces a lethal anemic phenotype, causing death by embryonic day 14, and natural mutations lead to β+ thalassemia in humans. However, expression of embryonic hemoglobin and fetal hemoglobin genes is normal in EKLF-deficient mice, and since all genes on the human β-globin locus exhibit the CACCC elements, researchers began searching for other Krüppel-like factors.
KLF2, initially called lung Krüppel-like Factor due to its high expression in the adult mouse lung, was first isolated in 1995 by using the zinc finger domain of EKLF as a hybridization probe. By transactivation assay in mouse fibroblasts, KLF2 was also noticed to bind to the β-globin gene promoter containing the CACCC sequence shown to be the binding site for EKLF, con |
https://en.wikipedia.org/wiki/RNPS1 | RNA-binding protein with serine-rich domain 1 is a protein that in humans is encoded by the RNPS1 gene.
Function
This gene encodes a protein that is part of a post-splicing multiprotein complex, the exon junction complex, involved in both mRNA nuclear export and mRNA surveillance. mRNA surveillance detects exported mRNAs with truncated open reading frames and initiates nonsense-mediated mRNA decay (NMD). When translation ends upstream from the last exon-exon junction, this triggers NMD to degrade mRNAs containing premature stop codons. This protein binds to the mRNA and remains bound after nuclear export, acting as a nucleocytoplasmic shuttling protein. This protein contains many serine residues. Two splice variants have been found for this gene; both variants encode the same protein.
Interactions
RNPS1 has been shown to interact with SART3 and Pinin.
References
Further reading
External links |
https://en.wikipedia.org/wiki/CD2AP | CD2-associated protein is a protein that in humans is encoded by the CD2AP gene.
Function
This gene encodes a scaffolding molecule that regulates the actin cytoskeleton. The protein directly interacts with filamentous actin and a variety of cell membrane proteins through multiple actin binding sites, SH3 domains, and a proline-rich region containing binding sites for SH3 domains. The cytoplasmic protein localizes to membrane ruffles, lipid rafts, and the leading edges of cells. It is implicated in dynamic actin remodeling and membrane trafficking that occurs during receptor endocytosis and cytokinesis. Haploinsufficiency of this gene is implicated in susceptibility to glomerular disease.
Interactions
CD2AP has been shown to interact with:
Cbl gene,
NPHS2,
Nephrin, and
RAB4A.
See also
Focal segmental glomerulosclerosis
References
Further reading
External links |
https://en.wikipedia.org/wiki/POT1 | Protection of telomeres protein 1 is a protein that in humans is encoded by the POT1 gene.
Function
This gene is a member of the telombin family and encodes a nuclear protein involved in telomere maintenance. Specifically, this protein functions as a member of a multi-protein complex known as shelterin, that binds to the TTAGGG repeats of telomeres, regulating telomere length and protecting chromosome ends from illegitimate recombination, catastrophic chromosome instability, and abnormal chromosome segregation. Alternatively spliced transcript variants have been described.
The absence of POT1 in mouse embryonic fibroblasts and chicken cells leads to a detrimental DNA damage response on telomeres resulting in telomere dysfunction-induced foci (TIFs). POT1 is required for telomere protection because it allows for telomere inhibition of DNA damage response factors. The protein also serves a role in the regulation of telomerase activity on telomeres. In vitro experiments utilizing human POT1 have shown that reduction in POT1 levels result in the elongation of telomeres.
Interactions
POT1 has been shown to interact with ACD and TINF2.
Pathology
Increased transcriptional expression of this gene is associated with stomach carcinogenesis and its progression.
Mutations in this gene have also been associated to the acquisition of the malignant features of chronic lymphocytic leukemia.
POT1 loss-of-function variants predispose to familial melanoma and glioma.
References
Fur |
https://en.wikipedia.org/wiki/UPF2 | Regulator of nonsense transcripts 2 is a protein that in humans is encoded by the UPF2 gene.
Function
This gene encodes a protein that is part of a post-splicing multiprotein complex, the exon junction complex, involved in both mRNA nuclear export and mRNA surveillance. mRNA surveillance detects exported mRNAs with truncated open reading frames and initiates nonsense-mediated mRNA decay (NMD). When translation ends upstream from the last exon-exon junction, this triggers NMD to degrade mRNAs containing premature stop codons. This protein is located in the perinuclear area. It interacts with translation release factors and the proteins that are functional homologs of yeast Upf1p and Upf3p. Two splice variants have been found for this gene; both variants encode the same protein. UPF2 has recently been shown to alter adult behavior via alterations in hippocampal synaptic spine density and the late long-term potentiation of neurons.
Interactions
UPF2 has been shown to interact with UPF1, UPF3A and UPF3B.
References
Further reading |
https://en.wikipedia.org/wiki/ARHGDIA | Rho GDP-dissociation inhibitor 1 is a protein that in humans is encoded by the ARHGDIA gene.
Interactions
ARHGDIA has been shown to interact with:
CDC42,
RAC1,
RHOA,
Rac2, and
RhoH.
References
External links
Further reading |
https://en.wikipedia.org/wiki/ATP2B2 | Plasma membrane calcium-transporting ATPase 2 is an enzyme that in humans is encoded by the ATP2B2 gene.
The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. This gene encodes the plasma membrane calcium ATPase isoform 2. Alternatively spliced transcript variants encoding different isoforms have been identified.
References
External links
Further reading |
https://en.wikipedia.org/wiki/ATP6V1E1 | V-type proton ATPase subunit E 1 is an enzyme that in humans is encoded by the ATP6V1E1 gene.
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. This gene encodes alternate transcriptional splice variants, encoding different V1 domain E subunit isoforms. Pseudogenes for this gene have been found in the genome.
References
External links
Further reading |
https://en.wikipedia.org/wiki/KCNJ6 | G protein-activated inward rectifier potassium channel 2 is a protein that in humans is encoded by the KCNJ6 gene. Mutation in KCNJ6 gene has been proposed to be the cause of Keppen-Lubinsky Syndrome (KPLBS).
Function
Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins and may be involved in the regulation of insulin secretion by glucose. It associates with two other G-protein-activated potassium channels to form a heteromultimeric pore-forming complex.
Interactions
KCNJ6 has been shown to interact with KCNJ9 and DLG1.
See also
G protein-coupled inwardly-rectifying potassium channel
Inward-rectifier potassium ion channel
References
Further reading
External links
Ion channels |
https://en.wikipedia.org/wiki/LGALS3BP | Galectin-3-binding protein is a protein that in humans is encoded by the LGALS3BP gene.
Function
The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell–cell and cell–matrix interactions. Using fluorescence in–situ hybridization, the full length 90K cDNA has been localized to chromosome 17q25. The native protein binds specifically to a human macrophage-associated lectin known as Mac-2 and also binds to galectin 1.
Clinical significance
LGALS3BP has been found elevated in the serum of patients with cancer and in those infected by the human immunodeficiency virus (HIV). It appears to be implicated in immune response associated with natural killer (NK) and lymphokine-activated killer (LAK) cell cytotoxicity.
Interactions
LGALS3BP has been shown to interact with LGALS3.
References
Further reading |
https://en.wikipedia.org/wiki/Lumican | Lumican, also known as LUM, is an extracellular matrix protein that, in humans, is encoded by the LUM gene on chromosome 12.
Structure
Lumican is a proteoglycan Class II member of the small leucine-rich proteoglycan (SLRP) family that includes decorin, biglycan, fibromodulin, keratocan, epiphycan, and osteoglycin.
Like the other SLRPs, lumican has a molecular weight of about 40 kiloDaltons and has four major intramolecular domains:
a signal peptide of 16 amino acid residues;
a negatively-charged N-terminal domain containing sulfated tyrosine and disulfide bond(s);
ten tandem leucine-rich repeats allowing lumican to bind to other extracellular components such as collagen;
a carboxyl terminal domain of 50 amino acid residues containing two conserved cysteines 32 residues apart.
There are four N-linked sites within the leucine-rich repeat domain of the protein core that can be substituted with keratan sulfate. The core protein of lumican (like decorin and fibromodulin) is horseshoe shaped. This enables it bind to collagen molecules within a collagen fibril, thus helping keep adjacent fibrils apart.
Function
Lumican is a major keratan sulfate proteoglycan of the cornea but is ubiquitously distributed in most mesenchymal tissues throughout the body. Lumican is involved in collagen fibril organization and circumferential growth, corneal transparency, and epithelial cell migration and tissue repair. Corneal transparency is possible due to the exact alignment of collagen |
https://en.wikipedia.org/wiki/MEF2D | Myocyte-specific enhancer factor 2D is a protein that in humans is encoded by the MEF2D gene.
Interactions
MEF2D has been shown to interact with:
CABIN1,
EP300,
MAPK7,
Myocyte-specific enhancer factor 2A,
NFATC2
Sp1 transcription factor, and
YWHAQ.
See also
Mef2
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/MSH3 | DNA mismatch repair protein, MutS Homolog 3 (MSH3) is a human homologue of the bacterial mismatch repair protein MutS that participates in the mismatch repair (MMR) system. MSH3 typically forms the heterodimer MutSβ with MSH2 in order to correct long insertion/deletion loops and base-base mispairs in microsatellites during DNA synthesis. Deficient capacity for MMR is found in approximately 15% of colorectal cancers, and somatic mutations in the MSH3 gene can be found in nearly 50% of MMR-deficient colorectal cancers.
Gene and expression
In humans, the encoding gene for MSH3 is found on chromosome 5 at location 5q11-q12 upstream of the dihydrofolate reductase (DHFR) gene. MSH3 is encoded by 222,341 base pairs and creates a protein consisting of 1137 amino acids.
MSH3 is typically expressed at low levels in several transformed cell lines—including HeLa, K562, HL-60, and CEM—as well as a large range of normal tissues including spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, heart, brain, placenta, lung, liver, skeletal muscle kidney, and pancreas. Although expression levels of MSH3 vary slightly from tissue to tissue, its widespread low-level expression indicates that it is a “housekeeping” gene commonly expressed in all cells.
Over-expression of MSH3 decreased capacity for MMR. When MSH3 is over expressed, drastic changes occur in the relative levels of formation of MutSβ at the expense of MutSα. MutSα is responsible for base-ba |
https://en.wikipedia.org/wiki/Metallothionein-3 | Metallothionein-3 (also known as Growth Inhibitory Factor) is a protein that in humans is encoded by the MT3 gene.
It is a 68-amino acid peptide (20 of which are cysteine) that is abnormally under-expressed in the brains of patients with Alzheimer's disease.
Metallothionein-3 is a member of the metallothionein family of proteins.
References
Further reading |
https://en.wikipedia.org/wiki/GADD45B | Growth arrest and DNA-damage-inducible, beta, also known as GADD45B, is a protein which in humans is encoded by the GADD45B gene.
Function
This gene is a member of a group of genes whose transcript levels are increased following stressful growth arrest conditions and treatment with DNA-damaging agents. The genes in this group respond to environmental stresses by mediating activation of the p38/JNK pathway. This activation is mediated via their proteins binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. The function of these genes or their protein products is involved in the regulation of growth and apoptosis. These genes are regulated by different mechanisms, but they are often coordinately expressed and can function cooperatively in inhibiting cell growth.
Gadd45b is required for activity-induced DNA demethylation of specific promoters and expression of corresponding genes necessary for adult neurogenesis, including brain-derived neurotrophic factor and fibroblast growth factor. Hence GADD45B is implicated in affecting synaptic plasticity.
Interactions
GADD45B has been shown to interact with:
ASK1,
GADD45GIP1,
MAP2K7 and
MAP3K4.
See also
Gadd45
References
Further reading |
https://en.wikipedia.org/wiki/SEPT2 | Septin 2, also known as SEPT2, is a protein which in humans is encoded by the SEPT2 gene.
Function
SEPT2 can hetero-oligomerize with SEPT6 and SEPT7 to form filaments. SEPT2 interacted with SEPT6 through its C-terminal coiled-coil domain. Knockdown of SEPT2, SEPT6, and SEPT7 in causes actin stress fibers to disintegrate and cells to lose polarity. Septins, SOCS7, and NCK1 are part of a signaling pathway that ties regulation of the DNA damage response to the cytoskeleton.
Interactions
SEPT2 has been shown to interact with:
SEPT6
SEPT7, and
SEPT9.
References
Further reading |
https://en.wikipedia.org/wiki/PEPD | Xaa-Pro dipeptidase, also known as prolidase, is an enzyme that in humans is encoded by the PEPD gene.
Function
Xaa-Pro dipeptidase is a cytosolic dipeptidase that hydrolyzes dipeptides with proline or hydroxyproline at the carboxy terminus (but not Pro-Pro). It is important in collagen metabolism because of the high levels of imino acids. Mutations at the PEPD locus cause prolidase deficiency. This is characterised by Iminodipeptidurea, skin ulcers, mental retardation and recurrent infections.
Structure
Prolidases fall under a subclass of metallopeptidases that involve binuclear active site metal clusters. This metal cluster facilitates catalysis by serving as a substrate binding site, activating nucleophiles, and stabilizing the transition state. Furthermore, prolidases are classified under a smaller family called “pita-bread” enzymes, which cleave amido-, imido-, and amidino- containing bonds. The “pita-bread” fold, containing a metal center flanked by two well-defined substrate binding pockets enabled prolidase to specifically cleave between any non-proline amino acid and proline.
The first ever solved structure of prolidase came from the hyperthermophilic archaeon Pyrococcus furiosus (Pfprol). This dimer has a crystal structure shows two approximately symmetrical monomers that both have an N-terminal domain, made up of a six-stranded mixed β-sheet flanked by five α-helices, a helical linker, and C-terminal domain, consisting of a mixed six-stranded β-sheet flanked |
https://en.wikipedia.org/wiki/PEX1 | Peroxisome biogenesis factor 1, also known as PEX1, is a protein which in humans is encoded by the PEX1 gene.
This gene encodes a member of the AAA protein family, a large group of ATPases associated with diverse cellular activities. This protein is cytoplasmic but is often anchored to a peroxisomal membrane where it forms a heteromeric complex and plays a role in the import of proteins into peroxisomes and peroxisome biogenesis. Mutations in this gene have been associated with complementation group 1 peroxisomal disorders such as neonatal adrenoleukodystrophy, infantile Refsum disease, and Zellweger syndrome.
Interactions
PEX1 has been shown to interact with PEX6 and PEX26.
Related diseases
Mutations in the genes encoding PEX1, along with PEX6, are the leading causes of peroxisomal biogenesis disorders, such as Zellweger Syndrome spectrum, infantile Refsum disease, and neonatal adrenoleukodystrophy. These genetic diseases are autosomal recessive and occur in 1 of every 50,000 births. Because of the autosomal recessive inheritance of Zellweger Syndrome, PEX1 is usually found in carrier screening gene panels. A very common PEX1 variant, Gly843Asp, is a mild allele well-reported in the literature.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Peroxisome Biogenesis Disorders, Zellweger Syndrome Spectrum
OMIM entries on Peroxisome Biogenesis Disorders, Zellweger Syndrome Spectrum |
https://en.wikipedia.org/wiki/PIK3C2A | Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing alpha polypeptide is an enzyme that in humans is encoded by the PIK3C2A gene.
The protein encoded by this gene belongs to the phosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles in signaling pathways involved in cell proliferation, oncogenic transformation, cell survival, cell migration, and intracellular protein trafficking.
This protein contains a lipid kinase catalytic domain as well as a C-terminal C2 domain, a characteristic of Class II PI 3-kinases. C2 domains act as calcium-dependent phospholipid binding motifs that mediate translocation of proteins to membranes, and may also mediate protein-protein interactions. The PI3-kinase activity of this protein is not sensitive to nanomolar levels of the inhibitor wortmannin. This protein was shown to be able to be activated by insulin and may be involved in integrin-dependent signaling.
Clinical significance
Three families have been reported with homozygous loss of function mutations in this gene. The clinical features of this syndrome include short stature, coarse facial features, cataracts with secondary glaucoma, multiple skeletal abnormalities and neurological manifestations. Abnormalities of cilial function were also noted.
References
Further reading
External links |
https://en.wikipedia.org/wiki/PTPRZ1 | Receptor-type tyrosine-protein phosphatase zeta also known as phosphacan is an enzyme that in humans is encoded by the PTPRZ1 gene.
Function
This gene is a member of the receptor tyrosine phosphatase family and encodes a single-pass type I membrane protein with two cytoplasmic tyrosine-protein phosphatase domains, an alpha-carbonic anhydrase domain and a fibronectin type III domain. Alternative splice variants that encode different protein isoforms have been described but their full-length nature has not been determined.
Clinical significance
Expression of this gene is induced in gastric cancer cells, in the remyelinating oligodendrocytes of multiple sclerosis lesions, and in human embryonic kidney cells under hypoxic conditions. Both the protein and transcript are overexpressed in glioblastoma cells, promoting their haptotactic migration.
References
Further reading
EC 3.1.3 |
https://en.wikipedia.org/wiki/PEX19 | Peroxisomal biogenesis factor 19 is a protein that in humans is encoded by the PEX19 gene.
Interactions
PEX19 has been shown to interact with:
ABCD1,
ABCD2,
ABCD3,
PEX10,
PEX11B,
PEX12,
PEX13,
PEX16, and
PEX3.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Peroxisome Biogenesis Disorders, Zellweger Syndrome Spectrum
OMIM entries on Peroxisome Biogenesis Disorders, Zellweger Syndrome Spectrum |
https://en.wikipedia.org/wiki/RAP2A | Ras-related protein Rap-2a is a protein that in humans is encoded by the RAP2A gene. RAP2A is a member of the Ras-related protein family.
Interactions
RAP2A has been shown to interact with RUNDC3A, RASSF5 and RALGDS.
References
Further reading |
https://en.wikipedia.org/wiki/RFC4 | Replication factor C subunit 4 is a protein that in humans is encoded by the RFC4 gene.
Function
The elongation of primed DNA templates by DNA polymerase delta and DNA polymerase epsilon requires the accessory proteins proliferating cell nuclear antigen (PCNA) and replication factor C (RFC). RFC, also named activator 1, is a protein complex consisting of five distinct subunits of 140, 40, 38, 37, and 36 kD. This gene encodes the 37 kD subunit. This subunit forms a core complex with the 36 and 40 kDa subunits. The core complex possesses DNA-dependent ATPase activity, which was found to be stimulated by PCNA in an in vitro system. Alternatively spliced transcript variants encoding the same protein have been reported.
Interactions
RFC4 has been shown to interact with:
BRD4,
CHTF18,
PCNA,
RFC2,
RFC3, and
RFC5.
References
Further reading |
https://en.wikipedia.org/wiki/Retinaldehyde-binding%20protein%201 | Retinaldehyde-binding protein 1 (RLBP1) also known as cellular retinaldehyde-binding protein (CRALBP) is a 36-kD water-soluble protein that in humans is encoded by the RLBP1 gene.
Discovery
Cellular retinol binding protein (CRBP) was first discovered in 1973 from lung tissues by Bashor et al. There have been three cellular retinol binding protein categories discovered; Cellular retinol-binding protein, cellular retinoic acid-binding protein and cellular retinaldehyde-binding protein(CRALBP). CRALBP was first discovered in 1977, after it was purified from retina and retinal pigment epithelial cells.
Function
The cellular retinaldehyde-binding protein transports 11-cis-retinal (also known as 11-cis-retinaldehyde) as its physiological ligands. It plays a critical role as an 11-cis-retinal acceptor which facilitates the enzymatic isomerization of all 11-trans-retinal to 11-cis-retinal, in the isomerization of the rod and cones of the visual cycle.
Tissue distribution
CRALBP is not just found in retina and retinal pigment epithelial cells, but also expressed in other cell types. It is majorly found in the iris, cornea, ciliary epithelium, Muller cells, the pineal gland and oligodendrocytes of the optic nerve and brain. This protein is also found in other tissues than the aforementioned ones, however its function in cells not related to the eyes are not yet known
Clinical significance
When a visual pigment molecule in photoreceptors of mammalian rod and cone cells are tri |
https://en.wikipedia.org/wiki/SATB1 | SATB1 (special AT-rich sequence-binding protein-1) is a protein which in humans is encoded by the SATB1 gene. It is a dimeric/tetrameric transcription factor with multiple DNA binding domains (CUT1, CUT2 and a Homeobox domain). SATB1 specifically binds to AT-rich DNA sequences with high unwinding propensity called base unpairing regions (BURs), containing matrix attachment regions (MARs).
Function
SATB1 is as a key factor for regulating spatial genome organization and subsequently integrating higher-order chromatin architecture with gene regulation. By binding to MARs and tethering these to the nuclear matrix, SATB1 creates chromatin loops. By changing the chromatin-loop architecture SATB1 is able to change gene transcription. The majority of SATB1 binding sites in the DNA are occupied by CTCF as well, another important chromatin organizer.
Immune system
SATB1 has a multitude of roles in the development of T cells.
SATB1 plays a role in controlling expression of lineage-specific factors during T cell development, including ThPOK, Runx3, CD4, CD8, and Treg factor Foxp3. SATB1-deficient thymocytes enter inappropriate T lineages and fail to generate the NKT and Treg subsets. The Treg deficiency subsequently causes an auto-immune phenotype in Satb1-deficient mouse models. The auto-immune phenotype is associated with loss of SATB1-dependent spatial rearrangement of the TCRα enhancer and the TCR locus, controlling TCR recombination via downregulation of the Rag1 and Rag2 g |
https://en.wikipedia.org/wiki/EGLN1 | Hypoxia-inducible factor prolyl hydroxylase 2 (HIF-PH2), or prolyl hydroxylase domain-containing protein 2 (PHD2), is an enzyme encoded by the EGLN1 gene. It is also known as Egl nine homolog 1. PHD2 is a α-ketoglutarate/2-oxoglutarate-dependent hydroxylase, a superfamily non-haem iron-containing proteins. In humans, PHD2 is one of the three isoforms of hypoxia-inducible factor-proline dioxygenase, which is also known as HIF prolyl-hydroxylase.
The hypoxia response
HIF-1α is a ubiquitous, constitutively synthesized transcription factor responsible for upregulating the expression of genes involved in the cellular response to hypoxia. These gene products may include proteins such as glycolytic enzymes and angiogenic growth factors. In normoxia, HIF alpha subunits are marked for the ubiquitin-proteasome degradation pathway through hydroxylation of proline-564 and proline-402 by PHD2. Prolyl hydroxylation is critical for promoting pVHL binding to HIF, which targets HIF for polyubiquitylation.
Structure
PHD2 is a 46-kDa enzyme that consists of an N-terminal domain homologous to MYND zinc finger domains, and a C-terminal domain homologous to the 2-oxoglutarate dioxygenases. The catalytic domain consists of a double-stranded β-helix core that is stabilized by three α-helices packed along the major β-sheet. The active site, which is contained in the pocket between the β-sheets, chelates iron(II) through histidine and aspartate coordination. 2-oxoglutarate displaces a water molecul |
https://en.wikipedia.org/wiki/ELAC2 | Zinc phosphodiesterase ELAC protein 2 is an enzyme that in humans is encoded by the ELAC2 gene. on chromosome 17. It is an endonuclease thought to be involved in mitochondrial tRNA maturation,
Function
The ELAC2 gene encodes a protein that is 92 kDa in size and is localized to the mitochondrion and the nucleus. The ELAC2 protein is a zinc phosphodiesterase, which is known to show tRNA 3'-processing endonuclease activity inside the mitochondria. Mitochondria contain their own pool of tRNAs that are involved in the protein translation of 13 subunits of the respiratory chain that are encoded by the mitochondrial genome. ELAC2 functions in the maturation of tRNA by removing a 3'-trailer (extra 3' nucleotides) from tRNA precursors, generating 3' termini of tRNAs.
The reaction leaves a 3'-hydroxy group is left at the tRNA end, and a 5'-phosphoryl group at the cleaved, trailing end. The reaction requires zinc ions as co-factors.
Clinical significance
Variants of the ELAC2 gene are associated with prostate cancer, hereditary 2 (HPC2), a condition associated with familial cancer of the prostate. Multiple mutations including truncation and missense mutations are known to cause the disease from multiple families based on linkage analysis and positional cloning.
In addition, mutations in ELAC2 are known to cause combined oxidative phosphorylation deficiency 17 (COXPD17), a rare autosomal recessive disorder of mitochondrial functions characterized by severe hypertrophic cardiomyop |
https://en.wikipedia.org/wiki/CA1%20%28gene%29 | Carbonic anhydrase 1 is an enzyme that in humans is encoded by the CA1 gene.
Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including cellular respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid.
They show extensive diversity in tissue distribution and in their subcellular localization. CA1 is closely linked to CA2 and CA3 genes on chromosome 8, and it encodes a cytosolic protein which is found at the highest level in erythrocytes. Transcript variants of CA1 utilizing alternative polyA_sites have been described in literature.
Structure
The human CA1 protein contains an N-terminus active site, zinc binding site, and substrate-binding site. The crystal structure of the human CA1-bicarbonate anion complex reveals the geometry of two H-bonds between the Glu106-Thr199 pair and the Glu117-His119 pair, and one pi H-bond between a water molecule and the phenyl ring of the Tyr114 residue. The product inhibition of CA1 via bicarbonate anions is correlated to the proton localization change on His119. So the Glu117-His119 H-bond is considered to regulate the ionicity of the zinc ion and the binding strength of the bicarbonate anion.
Mechanism
The reaction catalyzed by CA1 is the same as other carbonic anhydrase family proteins:
{CO2} + H2O ->[{}\atop\ce{ |
https://en.wikipedia.org/wiki/SFRS3 | Splicing factor, arginine/serine-rich 3 is a protein that in humans is encoded by the SFRS3 gene.
Browser View
UCSC Genome Browser View
UCSC Gene details page
Interactions
SFRS3 has been shown to interact with RBM7.
References
Further reading |
https://en.wikipedia.org/wiki/SGCB | Beta-sarcoglycan is a protein that in humans is encoded by the SGCB gene.
The dystrophin-glycoprotein complex (DGC) is a multisubunit protein complex that spans the sarcolemma and provides structural linkage between the subsarcolemmal cytoskeleton and the extracellular matrix of muscle cells. There are 3 main subcomplexes of the DGC: the cytoplasmic proteins dystrophin (DMD; MIM 300377) and syntrophin (SNTA1; MIM 601017), the alpha- and beta-dystroglycans (see MIM 128239), and the sarcoglycans (see, e.g., SGCA; MIM 600119) (Crosbie et al., 2000).[supplied by OMIM]
References
Further reading
External links
LOVD mutation database: SGCB |
https://en.wikipedia.org/wiki/SLC22A2 | Solute carrier family 22 member 2 (also termed OCT2 or organic cation transporter-2) is a protein that in humans is encoded by the SLC22A2 gene.
Polyspecific organic cation transporters in the liver, kidney, intestine, and other organs are critical for elimination of many endogenous small organic cations as well as a wide array of drugs and environmental toxins. This gene is one of three similar cation transporter genes located in a cluster on chromosome 6. The encoded protein contains twelve putative transmembrane domains and is a plasma integral membrane protein. It is found primarily in the kidney, where it may mediate the first step in cation reabsorption.
See also
Solute carrier family
References
Further reading
Solute carrier family |
https://en.wikipedia.org/wiki/SUMO3 | Small ubiquitin-related modifier 3 is a protein that in humans is encoded by the SUMO3 gene.
Function
SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002).[supplied by OMIM]
Interactions
SUMO3 has been shown to interact with ARNTL and Thymine-DNA glycosylase.
References
Further reading |
https://en.wikipedia.org/wiki/SOAT1 | Sterol O-acyltransferase (acyl-Coenzyme A: cholesterol acyltransferase) 1, also known as SOAT1, is an enzyme that in humans is encoded by the SOAT1 gene.
Function
Acyl-coenzyme A:cholesterol acyltransferase () is an intracellular protein located in the endoplasmic reticulum that forms cholesterol esters from cholesterol. Accumulation of cholesterol esters as cytoplasmic lipid droplets within macrophages and smooth muscle cells is a characteristic feature of the early stages of atherosclerotic plaques (Cadigan et al., 1988).
Structure and biogenesis
SOAT1 is a polytopic integral membrane protein belonging to the membrane-bound O-acyltransferase (MBOAT) superfamily. The structure of SOAT1 has not yet been solved but that of DltB, a bacterial MBOAT, suggests a complex arrangement of multiple transmembrane domains (TMDs). Primary sequences of predicted SOAT1 TMDs indicate many unusual TMD features such as the presence of multiple charged residues within the lipid bilayer. These features can render challenging the integration of a TMD into the hydrophobic phase of the membrane and might therefore require specialised chaperones. A first hint of such a chaperone assisting SOAT1 biogenesis has been the recognition of the involvement of the ER membrane protein complex (EMC), a molecular chaperone and insertase for integral membrane proteins, in maintaining SOAT1 stability.
Interactive pathway map
See also
Acyl-CoA:cholesterol acyltransferase
References
Further reading |
https://en.wikipedia.org/wiki/SON%20%28gene%29 | SON protein is a protein that in humans is encoded by the SON gene.
SON is the name that has been given to a large Ser/Arg (SR)-related protein, which is a splicing co-factor that contributes to an efficient splicing within cell cycle progression. It is also known as BASS1 (Bax antagonist selected in saccharomyces 1) or NRE-binding protein (Negative regulatory element-binding protein). The most common gene name of this splicing protein- which is only found in Humans (Homo sapiens)- is SON, but C21orf50, DBP5, KIAA1019 and NREBP can also be used as synonyms.
The protein encoded by SON gene binds to a specific DNA sequence upstream of the upstream regulatory sequence of the core promoter and second enhancer of human hepatitis B virus (HBV). Through this binding, it represses HBV core promoter activity, transcription of HBV genes, and production of HBV virions. The protein shows sequence similarities with other DNA-binding structural proteins such as gallin, oncoproteins of the MYC family, and the oncoprotein MOS. It may also be involved in protecting cells from apoptosis and in pre-mRNA splicing. Mutation in SON gene is associated with ZTTK syndrome.
Structure
The sequence length of the SON protein consists in 2426 aminoacids and its sequence status is totally completed. Its molecular weight is 263,830 Daltons (Da) and its domain contains 8 types of repeats which are distributed in 3 regions. This protein is found in the 21st chromosome and is mostly located in nuclear spe |
https://en.wikipedia.org/wiki/ST13 | Hsc70-interacting protein also known as suppression of tumorigenicity 13 (ST13) is a protein that in humans is encoded by the ST13 gene.
Function
The protein encoded by this gene is an adaptor protein that mediates the association of the heat shock proteins HSP70 and HSP90. This protein has been shown to be involved in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones. The expression of this gene is reported to be downregulated in colorectal carcinoma tissue suggesting that is a candidate tumor suppressor gene.
References
Further reading
Co-chaperones |
https://en.wikipedia.org/wiki/SULT1E1 | Estrogen sulfotransferase is an enzyme that in humans is encoded by the SULT1E1 gene.
Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes a protein that transfers a sulfo moiety to and from estrone, which may control levels of estrogen receptors.
See also
Steroidogenic enzyme
Steroid sulfotransferase
Estrone sulfotransferase
Steroid sulfatase
References
Further reading |
https://en.wikipedia.org/wiki/TAF2 | Transcription initiation factor TFIID subunit 2 is a protein that in humans is encoded by the TAF2 gene.
Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the larger subunits of TFIID that is stably associated with the TFIID complex. It contributes to interactions at and downstream of the transcription initiation site, interactions that help determine transcription complex response to activators.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/TAF10 | Transcription initiation factor TFIID subunit 10 is a protein that in humans is encoded by the TAF10 gene.
Function
Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the small subunits of TFIID that is associated with a subset of TFIID complexes. Studies with human and mammalian cells have shown that this subunit is required for transcriptional activation by the estrogen receptor, for progression through the cell cycle, and may also be required for certain cellular differentiation programs.
Interactions
TAF10 has been shown to interact with TAF9, Transcription initiation protein SPT3 homolog, TAF13 and TATA binding protein.
References
Further reading
External links |
https://en.wikipedia.org/wiki/TBX5%20%28gene%29 | T-box transcription factor TBX5, (T-box protein 5) is a protein that in humans is encoded by the TBX5 gene. Abnormalities in the TBX5 gene can result in altered limb development, Holt-Oram syndrome, Tetra-amelia syndrome, and cardiac and skeletal problems.
This gene is a member of a phylogenetically conserved family of genes that share a common DNA-binding domain, the T-box. T-box genes encode transcription factors involved in the regulation of developmental processes. This gene is closely linked to related family member T-box 3 (ulnar mammary syndrome) on human chromosome 12.
TBX5 is located on the long arm of chromosome 12. TBX5 produces a protein called T-box protein 5 that acts as a transcription factor. TBX5 is involved with forelimb and heart development. This gene impacts the early development of the forelimb by triggering fibroblast growth factor, FGF10.
Function
TBX5 is a transcription factor that codes for the protein called T-box 5. The transcription factors it encodes are necessary for development, especially in the pattern formation of upper limbs and cardiac growth. TBX5 is involved with the development of the four heart chambers, the electrical conducting system, and the septum separating the right and left sides of the heart. Along with playing roles in the development of the heart, septum, and electrical system of the heart, it also activates genes that are involved in the development of the upper limbs, the arms and hands.
This gene is also involved |
https://en.wikipedia.org/wiki/Deep%20Love | Deep Love is a Japanese cell phone novel series written by Yoshi, and is officially the first in its literary genre. The series includes four novels which were later published by Stars Publishing from December 2002 and July 2003. The series launched with Deep Love: Ayu no Monogatari, followed by Deep Love: Host, Deep Love: Reina no Unmei, and Deep Love: Pao no Monogatari.
After 2.6 million book copies were sold in Japan, the Deep Love novels were adapted into five manga series: three illustrated by Yū Yoshii, and one each drawn by Tetsu and Akiyo Kurosawa. Deep Love has also had two live-action series air on TV Tokyo: Ayu no Monogatari (2004) and Host (2005). A live-action film was released in theaters in 2004. Literary critic Minako Saitō panned the novels, suggesting that if it had been entered into a new writer competition in a literary magazine, it would have been rejected in the first round. She goes on to say that there might not even be any need to review such a work.
Synopsis
Ayu no Monogatari
This series follows Ayu, a high school girl who moonlights as a prostitute. She views the world as filthy, hypocritical, and hedonistic, and believes that money is the most important thing in the world. She lives with her boyfriend Kenji, a gigolo with a drug problem, and spends her school days with her friend Reina, her only friend.
Ayu's outlook on life changes after she meets an old woman, even going so far as to adopt Pao, an abused stray dog. However Ayu ends up betrayi |
https://en.wikipedia.org/wiki/ZNF148 | Zinc finger protein 148 is a protein that in humans is encoded by the ZNF148 gene.
Interactions
ZNF148 has been shown to interact with PTRF and P53.
See also
Zinc finger
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/HLA-B%20associated%20transcript%203 | Large proline-rich protein BAT3 is a protein that in humans is encoded by the BAT3 gene.
A cluster of genes, BAT1-BAT5, has been localized in the vicinity of the genes for TNF alpha and TNF beta. These genes are all within the human major histocompatibility complex class III region. The protein encoded by this gene is a nuclear protein. It has been implicated in the control of apoptosis and regulating heat shock protein. There are three alternatively spliced transcript variants described for this gene.
References
Further reading |
https://en.wikipedia.org/wiki/PABPN1 | Polyadenylate-binding protein 2 (PABP-2) also known as polyadenylate-binding nuclear protein 1 (PABPN1) is a protein that in humans is encoded by the PABPN1 gene. PABN1 is a member of a larger family of poly(A)-binding proteins in the human genome.
Function
This gene encodes an abundant nuclear protein that binds with high affinity to nascent poly(A) tails. The protein is required for progressive and efficient polymerization of poly(A) tails on the 3' ends of eukaryotic genes and controls the size of the poly(A) tail to about 250 nt. At steady-state, this protein is localized in the nucleus whereas a different poly(A) binding protein is localized in the cytoplasm. An expansion of the trinucleotide (GCN) repeat from normal 10 to 11-17 at the 5' end of the coding region of this gene leads to autosomal dominant oculopharyngeal muscular dystrophy (OPMD) disease. Multiple splice variants have been described but their full-length nature is not known. One splice variant includes introns 1 and 6 but no protein is formed.
Interactions
PABPN1 has been shown to interact with SNW1.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Oculopharyngeal Muscular Dystrophy
PDBe-KB provides an overview of all the structure information available in the PDB for Human Polyadenylate-binding protein 2 |
https://en.wikipedia.org/wiki/HIST1H4I | Histone H4 is a protein that, in humans, is encoded by the HIST1H4I gene.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H4 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the histone microcluster on chromosome 6p21.33.
References
Further reading |
https://en.wikipedia.org/wiki/NCK2 | Cytoplasmic protein NCK2 (also known as NCK-beta and Grb4) is a protein that in humans is encoded by the NCK2 gene.
Function
NCK belongs to family of adaptor proteins. There are two mammalian NCK genes, NCK1 and NCK2. NCK1 is located in chromosome 3 and NCK2 is located in chromosome 2. The protein contains three SH3 domains and one SH2 domain. The protein has no known catalytic function but has been shown to bind and recruit various proteins involved in the regulation of receptor protein tyrosine kinases. It is through these regulatory activities that this protein is believed to be involved in cytoskeletal reorganization. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Interactions
NCK2 has been shown to interact with:
Epidermal growth factor receptor,
LIMS1,
PDGFRB,
PTK2,
T-cell surface glycoprotein CD3 epsilon chain and
TrkB.
References
Further reading
External links
Nck2 Info with links in the Cell Migration Gateway
Human proteins |
https://en.wikipedia.org/wiki/Gem-associated%20protein%202 | Gem-associated protein 2 (GEMIN2), also called survival of motor neuron protein-interacting protein 1 (SIP1), is a protein that in humans is encoded by the GEMIN2 gene.
Interactions
Gem-associated protein 2 has been shown to interact with DDX20 and SMN1.
See also
Gideon Dreyfuss
Spinal muscular atrophy
References
Further reading |
https://en.wikipedia.org/wiki/AOC3 | Amine oxidase, copper containing 3 (AOC3), also known as vascular adhesion protein (VAP-1) and HPAO is an enzyme that in humans is encoded by the AOC3 gene on chromosome 17. This protein is a member of the semicarbazide-sensitive amine oxidase (SSAO; aka primary amine oxidase) family of enzymes and is associated with many vascular diseases.
Structure
VAP-1 is a type 1 membrane-bound glycoprotein that has a distal adhesion domain and an enzymatically active amine oxidase site outside of the membrane. The AOC3 gene is mapped onto 17q21 and has an exon count of 6.
Function
Amine oxidases are a family of enzymes that catalyze the oxidation of various endogenous amines, including histamine or dopamine. VAP-1 constitutes the copper dependent class of amine oxidases, such as lysyl oxidase or lysine demethylase, and is one of the four known in humans. The other class is flavin dependent such as monoamine oxidase (MAO) A and B. VAP-1, in particular, catalyzes the oxidative conversion of primary amines (methylamine and aminoacetone) to aldehydes (formaldehyde and methylglyoxal) ammonium and hydrogen peroxide in the presence of copper and quinone cofactor.
VAP-1 is primarily localized on the cell surface on the adipocyte plasma membrane. However, circulating VAP-1 has been shown to be the main source of SSAO in human serum. Serum VAP-1 originates from many tissues. VAP-1 has adhesive properties, functional monoamine oxidase activity, and possibly plays a role in glucose handling, |
https://en.wikipedia.org/wiki/BECN1 | Beclin-1 is a protein that in humans is encoded by the BECN1 gene. Beclin-1 is a mammalian ortholog of the yeast autophagy-related gene 6 (Atg6) and BEC-1 in the C. elegans nematode. This protein interacts with either BCL-2 or PI3k class III, playing a critical role in the regulation of both autophagy and cell death.
Role in disease
Beclin-1 plays an important role in tumorigenesis, and neurodegeneration, being implicated in the autophagic programmed cell death. Ovarian cancer with upregulated autophagy has a less aggressive behavior and is more responsive to chemotherapy.
Schizophrenia is associated with low levels of Beclin-1 in the hippocampus of those affected, which causes diminished autophagy which in turn results in increased neuronal cell death.
Interactions
BECN1 has been shown to interact with:
Bcl-2
BCL2L2
GOPC
MAP1LC3A
Rubicon
UVRAG
Modulators
Trehalose Trehalose reduces p62/Beclin-1 ratio and increases autophagy in the frontal cortex of ICR mice, possibly by increasing Beclin-1.
References
Further reading
External links
Genes
Human proteins |
https://en.wikipedia.org/wiki/Decoy%20receptor%202 | Decoy receptor 2 (DCR2), also known as TRAIL receptor 4 (TRAILR4) and tumor necrosis factor receptor superfamily member 10D (TNFRSF10D), is a human cell surface receptor of the TNF-receptor superfamily.
Function
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contains an extracellular TRAIL-binding domain, a transmembrane domain, and a truncated cytoplasmic death domain.
This receptor does not induce apoptosis, and has been shown to play an inhibitory role in TRAIL-induced cell apoptosis.
References
Further reading
Clusters of differentiation
TNF receptor family |
https://en.wikipedia.org/wiki/SOCS2 | Suppressor of cytokine signaling 2 is a protein that in humans is encoded by the SOCS2 gene.
This gene encodes a member of the STAT-induced STAT inhibitor (SSI), also known as suppressor of cytokine signalling (SOCS), family. SSI family members are cytokine-inducible negative regulators of cytokine signaling. The expression of this gene can be induced by a subset of cytokines, including erythropoietin, GM-CSF, IL10 and interferon-gamma (IFN-gamma). The protein encoded by this gene is found to interact with the cytoplasmic domain of insulin-like growth factor 1 receptor (IGF1R), and thus is thought to be involved in the regulation of IGF1R mediated cell signaling. Knockout studies in mice also suggested a regulatory role of this gene in IGF-1 related growth control.
Interactions
SOCS2 has been shown to interact with insulin-like growth factor 1 receptor and erythropoietin receptor. Additionally, it acts as a substrate recognition subunit of a Cullin5 E3 ubiquitin ligase complex. It is under investigation for use in targeted protein degradation.
References
Further reading
External links |
https://en.wikipedia.org/wiki/ADARB1 | Double-stranded RNA-specific editase 1 is an enzyme that in humans is encoded by the ADARB1 gene. The enzyme is a member of ADAR family.
Function
This gene encodes the enzyme responsible for pre-mRNA editing of the glutamate receptor subunit B by site-specific deamination of adenosines. Studies in rats found that this enzyme acted on its own pre-mRNA molecules to convert an AA dinucleotide to an AI dinucleotide which resulted in a new splice site. Alternative splicing of this gene results in several transcript variants, some of which have been characterized by the presence or absence of an Alu cassette insert and a short or long C-terminal region.
ADARB1 requires the small molecule inositol hexakisphosphate (IP6) for proper function. ADARB1 is an A-to-I RNA-editing enzyme that mostly acts on protein-coding substrates.
See also
Adenosine deaminase (ADA), an enzyme acting on isolated adenosine
References
Further reading
External links
EC 3.5 |
https://en.wikipedia.org/wiki/CDC34 | CDC34 is a gene that in humans encodes the protein Ubiquitin-conjugating enzyme E2 R1. This protein is a member of the ubiquitin-conjugating enzyme family, which catalyzes the covalent attachment of ubiquitin to other proteins.
CDC34 was originally discovered by work in baker's yeast as a gene that is essential for the cell cycle. Cdc34 in yeast targets numerous substrates - notably the cyclin-dependent kinase inhibitor Sic1 - for ubiquitin-mediated protein degradation. CDC34 is required for ubiquitin-mediated degradation of cell cycle G1 regulators, and for the initiation of DNA replication.
Interactions
CDC34 has been shown to interact with CSNK2B, BTRC and CDK9.
References
External links
Further reading |
https://en.wikipedia.org/wiki/CEBPE | CCAAT/enhancer binding protein (C/EBP), epsilon, also known as CEBPE and CRP1, is a type of ccaat-enhancer-binding protein. CEBPE is its human gene and is pro-apoptotic.
The protein encoded by this gene is a bZIP transcription factor which can bind as a homodimer to certain DNA regulatory regions. It can also form heterodimers with the related protein CEBP-δ. The encoded protein may be essential for terminal differentiation and functional maturation of committed granulocyte progenitor cells. Mutations in this gene have been associated with specific granule deficiency, a rare congenital disorder. Multiple variants of this gene have been described, but the full-length nature of only one has been determined.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/CPM%20%28gene%29 | Carboxypeptidase M is an enzyme that in humans is encoded by the CPM gene.
Function
The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene.
References
External links
Further reading |
https://en.wikipedia.org/wiki/CSTF2 | Cleavage stimulation factor 64 kDa subunit is a protein that in humans is encoded by the CSTF2 gene.
This gene encodes a nuclear protein with an RRM (RNA recognition motif) domain. The protein is a member of the cleavage stimulation factor (CSTF) complex that is involved in the 3' end cleavage and polyadenylation of pre-mRNAs. Specifically, this protein binds GU-rich elements within the 3'-untranslated region of mRNAs.
Interactions
CSTF2 has been shown to interact with CSTF3, SUB1, SYMPK, BARD1 and BRCA1.
References
External links
Further reading |
https://en.wikipedia.org/wiki/Cathepsin%20E | Cathepsin E is an enzyme () that in humans is encoded by the CTSE gene. The enzyme is also known as slow-moving proteinase, erythrocyte membrane aspartic proteinase, SMP, EMAP, non-pepsin proteinase, cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme.
Cathepsin E is a protease found in animals, as well as various other organisms, that belongs to the aspartic protease group. In humans it is encoded by the CTSE gene located at 1q32 on chromosome 1. It is an intracellular non-lysosomal glycoprotein that is mainly found in the skin and in immune cells. The protein is an aspartyl protease that functions as a disulfide-linked homodimer, and has an oligosaccharide chain of the high-mannose type. It is a member of the peptidase A1 family, and therefore observes specificity similar to that of Pepsin A and Cathepsin D. Cathepsin E is an intracellular enzyme and does not appear to be involved in dietary protein digestion. It is found at highest abundance on the stomach’s epithelial mucus producing cell surfaces. It is the first aspartic protease present in the fetal stomach and is found in more than half of gastric cancers, leading to it appearing to be an oncofetal antigen. Transcript variants utilizing alternative polyadenylation signals and two transcript variants encoding different isoforms exist for this gene.
A deficiency in the levels of Cathepsin E in the body may play a part in inflammatory skin diseases such as atopi |
https://en.wikipedia.org/wiki/DSC2 | Desmocollin-2 is a protein that in humans is encoded by the DSC2 gene. Desmocollin-2 is a cadherin-type protein that functions to link adjacent cells together in specialized regions known as desmosomes. Desmocollin-2 is widely expressed, and is the only desmocollin isoform expressed in cardiac muscle, where it localizes to intercalated discs. Mutations in DSC2 have been causally linked to arrhythmogenic right ventricular cardiomyopathy.
Structure
Desmocollin-2 is a calcium-dependent glycoprotein that is a member of the desmocollin subfamily of the cadherin superfamily. Three different posttranslational modifications (N-Glycosylations, O-Mannosylations and disulfide bridges) were present in the extracellular domain of desmocollin-2. The desmocollin family members are arranged as closely linked genes on human chromosome 18q12.1. Human DSC2 consists of greater than 32 kb of DNA and has 17 exons, with exon 16 being alternatively spliced and encoding distinct isoforms. Desmocollin-2 contains five N-terminal extracellular domains, a transmembrane-spanning domain, and a C-terminal cytoplasmic tail. Desmocollin-2 binds to desmoglein family members through a calcium-dependent interaction with its extracellular domains, and to plakoglobin through its cytoplasmic tail. Desmocollin-2 is ubiquitously expressed in desmosomal tissues, such as skin epithelia, and is the only desmocollin isoform expressed in human cardiac muscle, where it localizes to desmosomes within intercalated discs. |
https://en.wikipedia.org/wiki/LDB1 | LIM domain-binding protein 1 is a protein that in humans is encoded by the LDB1 gene.
Interactions
LDB1 has been shown to interact with LMO4, TCF3, TAL1 and CBFA2T3.
References
Further reading |
https://en.wikipedia.org/wiki/MED14 | Mediator of RNA polymerase II transcription subunit 14 is an enzyme that in humans is encoded by the MED14 gene.
The activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The protein encoded by this gene is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. This protein contains a bipartite nuclear localization signal. This gene is known to escape chromosome X-inactivation.
Interactions
MED14 has been shown to interact with PPARGC1A, Estrogen receptor alpha, STAT2, Cyclin-dependent kinase 8, Glucocorticoid receptor and Hepatocyte nuclear factor 4 alpha.
References
Further reading |
https://en.wikipedia.org/wiki/HOMER1 | Homer protein homolog 1 or Homer1 is a neuronal protein that in humans is encoded by the HOMER1 gene. Other names are Vesl and PSD-Zip45.
Structure
Homer1 protein has an N-terminal EVH1 domain, involved in protein interaction, and a C-terminal coiled-coil domain involved in self association. It consists of two major splice variants, short-form (Homer1a) and long-form (Homer1b and c). Homer1a has only EVH1 domain and is monomeric while Homer1b and 1c have both EVH1 and coiled-coil domains and are tetrameric. The coiled-coil can be further separated into N-terminal half and C-terminal half. The N-terminal half of the coiled-coil domain is predicted to be a parallel dimer while the C-terminus half is a hybrid of dimeric and anti-parallel tetrameric coiled-coil. As a whole, long Homer is predicted to have a dumbbell-like structure where two pairs of EVH1 domains are located on two sides of long (~50 nm) coiled-coil domain. Mammals have Homer2 and Homer3, in addition to Homer1, which have similar domain structure. They also have similar alternatively spliced forms.
Tissue distribution
Homer1 is expressed widely in the central nervous system as well as peripheral tissue including heart, kidney, ovary, testis, and skeletal muscle. Subcellularly in neurons, Homer1 is concentrated in postsynaptic structures and constitutes a major part of the postsynaptic density.
Function
EVH1 domain interacts with PPXXF motif. This sequence motif exists in group 1 metabotrophic gl |
https://en.wikipedia.org/wiki/H2AFY | Core histone macro-H2A.1 is a protein that in humans is encoded by the H2AFY gene.
Function
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene encodes a member of the histone H2A family. It replaces conventional H2A histones in a subset of nucleosomes where it represses transcription and participates in stable X chromosome inactivation. Alternative splicing results in multiple transcript variants encoding different isoforms. Expression of these isoforms is associated to several cancers, such as hepatocellular carcinoma.
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Core histone macro-H2A.1 |
https://en.wikipedia.org/wiki/SNCAIP | Synphilin-1 is a protein that in humans is encoded by the SNCAIP gene. SNCAIP stands for "synuclein, alpha interacting protein" and can be signified by SNCAP_HUMAN, synphilin 1, synuclein, alpha interacting protein (synphilin), and SYPH1.
Function
This gene encodes a protein containing several protein-protein interaction domains, including ankyrin-like repeats, a coiled-coil domain, and an ATP/GTP-binding motif. The encoded protein interacts with alpha-synuclein in neuronal tissue and may play a role in the formation of cytoplasmic inclusions and neurodegeneration. A mutation in this gene has been associated with Parkinson's disease. Alternatively spliced transcript variants encoding different isoforms of this gene have been described, but their full-length nature has yet to be determined.
The SNCAIP gene provides instructions for making a protein called synphilin-1 and a slightly different version of this protein called synphilin-1A. These proteins are produced in the brain. They are usually located in specialized structures called presynaptic terminals, found at the tips of nerve cells. In nerve cells, synphilin-1 and synphilin-1A interact with another protein called alpha-synuclein. The functions of synphilin-1 and synphilin-1A, however, are unknown.
Interactions
SNCAIP has been shown to interact with:
Alpha-synuclein and
Parkin (ligase).
References
Further reading |
https://en.wikipedia.org/wiki/CHAF1A | Chromatin assembly factor 1 subunit A is a protein that in humans is encoded by the CHAF1A gene.
Function
Chromatin assembly factor I (CAF-1) is a nuclear complex consisting of p50, p60 (CHAF1B; MIM 601245), and p150 (CHAF1A) subunits that assembles histone tetramers onto replicating DNA in vitro (Kaufman et al., 1995).[supplied by OMIM]
Interactions
CHAF1A has been shown to interact with:
ASF1A,
ASF1B,
BLM,
CBX5, and
MBD1.
References
Further reading
External links |
https://en.wikipedia.org/wiki/DPP3 | Dipeptidyl-peptidase 3 is an enzyme that in humans is encoded by the DPP3 gene.
This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Increased activity of this protein is associated with endometrial and ovarian cancers. Alternate transcriptional splice variants have been characterized.
References
Further reading
External links |
https://en.wikipedia.org/wiki/AKAP9 | A-kinase anchor protein 9 is a protein that in humans is encoded by the AKAP9 gene. AKAP9 is also known as Centrosome- and Golgi-localized protein kinase N-associated protein (CG-NAP) or AKAP350 or AKAP450
Function
The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family. Alternate splicing of this gene results in many isoforms that localize to the centrosome and the Golgi apparatus, and interact with numerous signaling proteins from multiple signal transduction pathways. These signaling proteins include type II protein kinase A, serine/threonine kinase protein kinase N, protein phosphatase 1, protein phosphatase 2a, protein kinase C-epsilon and phosphodiesterase 4D3.
Model organisms
Model organisms have been used in the study of AKAP9 function. A conditional knockout mouse line, called Akap9tm1a(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 six tests were carried out on mutant mice and eight significant abnormalities were observed. Fewer than expected homozygous mutant m |
https://en.wikipedia.org/wiki/G3BP1 | Ras GTPase-activating protein-binding protein 1 is an enzyme that in humans is encoded by the G3BP1 gene.
This gene encodes one of the DNA-unwinding enzymes which prefers partially unwound 3'-tailed substrates and can also unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. This enzyme is a member of the heterogeneous nuclear RNA-binding proteins and is also an element of the Ras signal transduction pathway. It was originally reported to bind specifically to the Ras-GTPase-activating protein by associating with its SH3 domain, but this interaction has recently been challenged. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.
G3BP1 can initiate stress granule formation and labeled G3BP1 is commonly used as a marker for stress granules.
Interactions
G3BP1 has been shown to interact with USP10.
It also interacts with SND1[5].
References
[5]Gao X, Ge L, Shao J, Su C, Zhao H, Saarikettu J, Yao X, Yao Z, Silvennoinen O, Yang J., Tudor-SN interacts with and co-localizes with G3BP in stress granules under stress conditions.FEBS Letters, Volume 584, Issue 16, Pages 3525-3532.
Further reading
External links |
https://en.wikipedia.org/wiki/IRF9 | Interferon regulatory factor 9 is a protein that in humans is encoded by the IRF9 gene, previously known as ISGF3G.
Interactions
IRF9 has been shown to interact with STAT2 and STAT1.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/TAB1 | Mitogen-activated protein kinase kinase kinase 7-interacting protein 1 is an enzyme that in humans is encoded by the TAB1 gene.
Function
The protein encoded by this gene was identified as a regulator of the MAP kinase kinase kinase MAP3K7/TAK1, which is known to mediate various intracellular signaling pathways, such as those induced by TGF-beta, interleukin-1, and WNT-1. This protein interacts and thus activates TAK1 kinase. It has been shown that the C-terminal portion of this protein is sufficient for binding and activation of TAK1, while a portion of the N-terminus acts as a dominant-negative inhibitor of TGF beta, suggesting that this protein may function as a mediator between TGF beta receptors and TAK1. This protein can also interact with and activate the mitogen-activated protein kinase 14 (MAPK14/p38alpha), and thus represents an alternative activation pathway, in addition to the MAPKK pathways, which contributes to the biological responses of MAPK14 to various stimuli. Alternatively spliced transcript variants encoding distinct isoforms have been reported. TAB1 contains multiple amino acid sites that are phosphorylated and ubiquitinated.
This protein plays an important role in skin homeostasis, wound repair, and oncogenesis.
Interactions
TAB1 has been shown to interact with:
MAP3K7IP2,
MAP3K7IP3,
MAP3K7,
MAP3K1,
MAPK14,
Mothers against decapentaplegic homolog 7,
TRAF6,
XIAP, and
ZMYND11.
References
Further reading |
https://en.wikipedia.org/wiki/DCTN2 | Dynactin subunit 2 is a protein that in humans is encoded by the DCTN2 gene
Function
This gene encodes a 50-kD subunit of dynactin, a macromolecular complex consisting of 23 subunits (11 individual proteins ranging in size from 22 to 150 kD). The subunit is commonly referred to as p50 or dynamitin. Dynactin binds to both microtubules and cytoplasmic dynein. It is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. This subunit is present in 4 copies per dynactin molecule. It contains three short alpha-helical coiled-coil domains that bind to two copies of p150-glued (DCTN1) and two copies of p24 (DCTN3) to form the dynactin shoulder domain.
Interactions
DCTN2 has been shown to interact with MARCKSL1.
References
Further reading |
https://en.wikipedia.org/wiki/ARL6IP5 | PRA1 family protein 3 is a protein that in humans is encoded by the ARL6IP5 gene.
Function
Expression of this gene is affected by vitamin A. The encoded protein of this gene may be associated with the cytoskeleton. A similar protein in rats may play a role in the regulation of cell differentiation. The rat protein binds and inhibits the cell membrane glutamate transporter EAAC1. The expression of the rat gene is upregulated by retinoic acid, which results in a specific reduction in EAAC1-mediated glutamate transport. The disruption of the mouse gene results in increased neuronal glutathione content, neuroprotection against oxidative stress and a better performance in motor/spatial learning and memory tests than wild-type mice.
Interactions
ARL6IP5 has been shown to interact with SLC1A1.
References
External links
Further reading |
https://en.wikipedia.org/wiki/TXNIP | Thioredoxin-interacting protein is a protein that in humans is encoded by the TXNIP gene.
Interactions
TXNIP has been shown to interact with Thioredoxin and ZBTB32.
Related gene problems
TAR syndrome
1q21.1 deletion syndrome
1q21.1 duplication syndrome
References
Further reading |
https://en.wikipedia.org/wiki/WNT3A | Protein Wnt-3a is a protein that in humans is encoded by the WNT3A gene.
The WNT gene family consists of structurally related genes that encode secreted signaling proteins. These proteins have are critical in tissue homeostasis, embryonic development, and disease.
Signaling and Related Genes
WNT3A is highly related to the WNT3 gene in sequence and protein function. WNT3A and WNT3 signal similarly through primarily the beta-catenin/Tcf pathway. WNT3A is located in the genome beside the WNT9A gene across many vertebrates. Similarly, the WNT3 gene occurs in the genome beside the WNT9B gene. WNT9A and WNT9B signal through the beta-catenin/Tcf pathway but do not play related roles as WNT3A and WNT3 in the same cellular processes.
Role in Disease
WNT3A is not linked to particular genetic disorder in humans. Mice that have a genetic mutation in the WNT3A die during early embryogenesis and fail to correctly form axial tissues. Wnt-3a promotes the beta-catenin/Tcf pathway which is tumor inducing and can cause cancer when expressed in particular cell populations.
Role in embryonic development
Embryonic development is the process where the body plan is created. From studies in vertebrate model systems we can infer the roles of particular genes in human anatomical structures. Wnt3a plays a role in these processes:
Body plan - Torso
Wnt3A patterns a multipotent stem cell population that form neurons, muscles, bones, and cartilage of the torso region. Wnt3a instructs these |
https://en.wikipedia.org/wiki/BAFF%20receptor | BAFF receptor (B-cell activating factor receptor, BAFF-R), also known as tumor necrosis factor receptor superfamily member 13C (TNFRSF13C) and BLyS receptor 3 (BR3), is a membrane protein of the TNF receptor superfamily which recognizes BAFF, an essential factor for B cell maturation and survival. In humans it is encoded by the TNFRSF13C gene.
Function
B-cell activating factor (BAFF) enhances B-cell survival in vitro and is a regulator of the peripheral B-cell population. The protein encoded by this gene is a receptor for BAFF and is a type III transmembrane protein containing a single extracellular phenylalanine-rich domain. It is thought that this receptor is the principal receptor required for BAFF-mediated mature B-cell survival. In B cell maturation, due to regulation by BAFF-R, only a limited amount of B-cell will survive.
Clinical significance
Overexpression of BAFF in mice results in mature B-cell hyperplasia and symptoms of systemic lupus erythematosus (SLE). Also, some SLE patients have increased levels of BAFF in serum. Therefore, it has been proposed that abnormally high levels of BAFF may contribute to the pathogenesis of autoimmune diseases by enhancing the survival of autoreactive B cells, which are cells that show immune response to normal body cells. Autoreactive B cells are less sensitive toward BAFF and are usually outcompeted by the normal B cells in the maturation process regulated by low BAFF-R expression. An elevated level of BAFF-R can therefore |
https://en.wikipedia.org/wiki/APLP1 | Amyloid-like protein 1, also known as APLP1, is a protein that in humans is encoded by the APLP1 gene. APLP1 along with APLP2 are important modulators of glucose and insulin homeostasis.
Function
This gene encodes a member of the highly conserved amyloid precursor protein gene family. The encoded protein is a membrane-associated glycoprotein that is cleaved by secretases in a manner similar to amyloid beta A4 precursor protein cleavage. This cleavage liberates an intracellular cytoplasmic fragment that may act as a transcriptional activator. The encoded protein may also play a role in synaptic maturation during cortical development. Alternatively spliced transcript variants encoding different isoforms have been described.
APLP1 and APLP2 double knockout mice display hypoglycemia and hyperinsulinemia indicating that these two proteins are important modulators of glucose and insulin homeostasis.
References
External links
Further reading |
https://en.wikipedia.org/wiki/Fibroblast%20growth%20factor%208 | Fibroblast growth factor 8 (FGF-8) is a protein that in humans is encoded by the FGF8 gene.
Function
The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion.
FGF-8 is important and necessary for setting up and maintaining the midbrain/hindbrain border (or mesencephalon/metencephalon border) which plays the vital role of “organizer” in development, like the Spemann organizer” of the gastrulating embryo. FGF-8 is expressed in the region where Otx2 and Gbx2 cross inhibit each other and is maintained expression by this interaction. Once expressed, the Fgf8 induces other transcription factors to form cross-regulatory loops between cells, thus the border is established. Through development, the Fgf8 goes to regulate the growth and differentiation of progenitor cells in this region to produce ultimate structure of midbrain and hindbrain. Crossely’s experiment proves that the FGF-8 is sufficient to induce the repatterning of midbrain and hindbrain structure.
In the development of forebrain, cortical patterning centers are the boundaries or poles of cortical primordium, where multiple BMP and WNT genes are expressed. Besides, at the anterior pole several FGF family including Fgf3, 8,17 and 18 overlap in expression. The |
https://en.wikipedia.org/wiki/FLNB | Filamin B, beta (FLNB), also known as Filamin B, beta (truncated actin binding protein 278 homolog), is a cytoplasmic protein which in humans is encoded by the FLNB gene.
FLNB regulates intracellular communication and signalling by cross-linking the protein actin to allow direct communication between the cell membrane and cytoskeletal network, to control and guide proper skeletal development.
Mutations in the FLNB gene are involved in several lethal bone dysplasias, including boomerang dysplasia and atelosteogenesis type I.
Interactions
FLNB has been shown to interact with GP1BA, Filamin, FBLIM1, PSEN1, CD29 and PSEN2.
See also
Larsen syndrome
References
External links
GeneReview/NIH/UW entry on FLNB-Related Disorders
Further reading |
https://en.wikipedia.org/wiki/GFER | Growth factor, augmenter of liver regeneration (ERV1 homolog, S. cerevisiae), also known as GFER, or Hepatopoietin is a protein which in humans is encoded by the GFER gene. This gene is also known as essential for respiration and vegatative growth, augmenter of liver regeneration, and growth factor of Erv1-like/Hepatic regenerative stimulation substance.
Structure
The GFER gene is located on the p arm of chromosome 16 at position 13.3 and it spans 3,600 base pairs. The GFER gene produces a 15.4 kDa protein composed of 130 amino acids. The structure of the protein is a homodimer which has been found to be fairly similar to the scERV1 protein of yeast.
Genomics
The gene resides on chromosome 16 in the interval containing the locus for polycystic kidney disease (PKD1). The putative gene product is 42% similar to the scERV1 protein of yeast. The human gene has three exons: the first encodes a 5' untranslated region and the first part of the protein; the second encodes the bulk of the protein; and the third the remainder.
Molecular biology
Proteins of the ERV1/ALR family are encoded by all eukaryotes and cytoplasmic DNA viruses for which the sequence data are available. All possess a C-X-X-C motif within a ~100 amino acid domain
Function
The hepatotrophic factor designated augmenter of liver regeneration (ALR) is thought to be one of the factors responsible for the extraordinary regenerative capacity of mammalian liver. It has also been called hepatic regenerative stimu |
https://en.wikipedia.org/wiki/HNRPH1 | Heterogeneous nuclear ribonucleoprotein H is a protein that in humans is encoded by the HNRNPH1 gene.
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has three repeats of quasi-RRM domains that bind to RNAs. It is very similar to the family member HNRPF. This gene is thought to be potentially involved in hereditary lymphedema type I phenotype.
References
Further reading |
https://en.wikipedia.org/wiki/AGFG1 | Arf-GAP domain and FG repeat-containing protein 1 is a protein that in humans is encoded by the AGFG1 gene.
Function
The protein encoded by this gene is related to nucleoporins, a class of proteins that mediate nucleocytoplasmic transport. This encoded protein binds the Rev activation domain when Rev is assembled onto its RNA target and can significantly enhance Rev activity when overexpressed. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.
Interactions
AGFG1 has been shown to interact with EPS15L1 and EPS15.
References
Further reading |
https://en.wikipedia.org/wiki/ICA1 | Islet cell autoantigen 1 is a protein that in humans is encoded by the ICA1 gene.
This gene encodes a protein with an arfaptin homology domain that is found both in the cytosol and as membrane-bound form on the Golgi complex and immature secretory granules. This protein is believed to be an autoantigen in insulin-dependent diabetes mellitus and primary Sjögren's syndrome. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.
References
Further reading |
https://en.wikipedia.org/wiki/IGKC | Immunoglobulin kappa constant, also known as IGKC, is a human gene that encodes the constant domain of kappa-type light chains for antibodies. It is found on chromosome 2, in humans, within the Immunoglobulin kappa locus, IGK@.
References
Further reading
Proteins |
https://en.wikipedia.org/wiki/IL1RAP | Interleukin-1 receptor accessory protein is a protein that in humans is encoded by the IL1RAP gene.
Interleukin 1 induces synthesis of acute phase and proinflammatory proteins during infection, tissue damage, or stress, by forming a complex at the cell membrane with an interleukin 1 receptor and an accessory protein. This gene encodes an interleukin 1 receptor accessory protein. Alternative splicing of this gene results in two transcript variants encoding two different isoforms, one membrane-bound and one soluble.
Interactions
IL1RAP has been shown to interact with TOLLIP and Interleukin 1 receptor, type I.
References
Further reading
External links
Proteins |
https://en.wikipedia.org/wiki/Interleukin%2015%20receptor%2C%20alpha%20subunit | Interleukin 15 receptor, alpha subunit is a subunit of the interleukin 15 receptor that in humans is encoded by the IL15RA gene.
Structure
The IL-15 receptor is composed of three subunits: IL-15R alpha, CD122, and CD132. Two of these subunits, CD122 and CD132, are shared with the receptor for IL-2, but IL-2 receptor has an additional subunit (CD25). The shared subunits contain the cytoplasmic motifs required for signal transduction, and this forms the basis of many overlapping biological activities of IL15 and IL2, although in vivo the two cytokines have separate biological effects. This may be due to effects of the respective alpha chains, which are unique to each receptor, the kinetics and affinity of cytokine-cytokine receptor binding, or due to the availability and concentration of each cytokine.
Function
IL-15Ralpha specifically binds IL15 with very high affinity, and is capable of binding IL-15 independently of other subunits. It is suggested that this property allows IL-15 to be produced by one cell, endocytosed by another cell, and then presented to a third party cell.
This receptor is reported to enhance cell proliferation and expression of apoptosis inhibitor BCL2L1/BCL2-XL and BCL2. Multiple alternatively spliced transcript variants of this gene have been reported. The full length sequences of only two variants encoding distinct isoforms are available.
Isoforms
Several isoforms of the IL-15Ralpha protein have been detected. These isoforms can either r |
https://en.wikipedia.org/wiki/IRF5 | Interferon regulatory factor 5 is a protein that in humans is encoded by the IRF5 gene. The IRF family is a group of transcription factors that are involved in signaling for virus responses in mammals along with regulation of certain cellular functions.
Function
IRF5 is a member of the interferon regulatory factor (IRF) family, a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats. Alternative splice variants encoding different isoforms exist. The regulatory and repression regions of the IRF family are mainly located in the C-terminal of the IRF.
A 2020 study showed that an adaptor protein named TASL play an important regulatory role in IRF5 activation by being phosphorylated at the pLxIS motif, drawing a similar analogy to the IRF3 activation pathway through the adaptor proteins MAVS, STING and TRIF.
Clinical significance
IRF5 acts as a molecular switch that controls whether macrophages will promote or inhibit inflammation. Blocking the production of IRF5 in macrophages may help treat a wide range of autoimmune diseases, and that boosting IRF5 levels might help treat people whose immune systems are weak, compromised, or damaged. IRF5 seems to work "either by interacting with DNA directly, or by interacting with o |
https://en.wikipedia.org/wiki/ITIH1 | Inter-alpha-trypsin inhibitor heavy chain H1 is a protein that in humans is encoded by the ITIH1 gene.
See also
Inter-alpha-trypsin inhibitor
ITIH2
ITIH3
ITIH4
References
Further reading |
https://en.wikipedia.org/wiki/KARS%20%28gene%29 | Lysyl-tRNA synthetase is an enzyme that in humans is encoded by the KARS gene.
Function
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Lysyl-tRNA synthetase is a homodimer localized to the cytoplasm which belongs to the class II family of tRNA synthetases. It has been shown to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis
Besides its role in translation, Lysyl-tRNA synthetase is involved in a signaling pathway leading to gene activation. Following physiological stimulation of a variety of cells, Lysyl-tRNA synthetase binds to the transcription factors MITF and USF2 and can then influence their transcriptional activities. Such physiological stimulation includes immunological activation of mast cells, so this pathway maybe relevant to the allergic response.
Interactions
KARS (gene) has been shown to interact with Multisynthetase complex auxiliary component p38. Physiological trigger such as immunological activation results in the phosphorylation of LysRS on its serine residues. It separates from the multisynthetase complex and initiates Ap4A production.
References
Further reading |
https://en.wikipedia.org/wiki/KTN1 | Kinectin is a protein that in humans is encoded by the KTN1 gene.
Function
Various cellular organelles and vesicles are transported along the microtubules in the cytoplasm. Likewise, membrane recycling of the endoplasmic reticulum (ER), Golgi assembly at the microtubule organizing center, and alignment of lysosomes along microtubules are all related processes. The transport of organelles requires a special class of microtubule-associated proteins (MAPs). One of these is the molecular motor kinesin (see MIM 148760 and MIM 600025), an ATPase that moves vesicles unidirectionally toward the plus end of the microtubule. Another such MAP is kinectin, a large integral ER membrane protein. Antibodies directed against kinectin have been shown to inhibit its binding to kinesin.[supplied by OMIM]
Interactions
KTN1 has been shown to interact with EEF1D, RhoG and RHOA.
References
Further reading |
https://en.wikipedia.org/wiki/TACSTD2 | Tumor-associated calcium signal transducer 2, also known as Trop-2 and as epithelial glycoprotein-1 antigen (EGP-1), is a protein that in humans is encoded by the TACSTD2 gene.
This intronless gene encodes a carcinoma-associated antigen defined by the monoclonal antibody GA733. This antigen is a member of a family including at least two type I membrane proteins. It transduces an intracellular calcium signal and acts as a cell surface receptor.
Mutations of this gene result in gelatinous drop-like corneal dystrophy, an autosomal recessive disorder characterized by severe corneal amyloidosis leading to blindness.
Trop-2 expression was originally described in trophoblasts (placenta) and fetal tissues (e.g., lung). Later, its expression was also described in the normal stratified squamous epithelium of the skin, uterine cervix, esophagus, and tonsillar crypts.
Trop-2 plays a role in tumor progression by actively interacting with several key molecular signaling pathways traditionally associated with cancer development and progression. Aberrant overexpression of Trop-2 has been described in several solid cancers, such as colorectal, renal, lung, and breast cancers. Trop-2 expression has also been described in some rare and aggressive malignancies, e.g., salivary duct, anaplastic thyroid, uterine/ovarian, and neuroendocrine prostate cancers.
This antigen is the target of sacituzumab govitecan, an antibody-drug conjugate.
References
Further reading |
https://en.wikipedia.org/wiki/CHST6 | Carbohydrate sulfotransferase 6 is an enzyme that in humans is encoded by the CHST6 gene.
It codes for an enzyme necessary for the production of keratan sulfate. Mutations in the gene lead to macular corneal dystrophy.
References
External links
Further reading |
https://en.wikipedia.org/wiki/DNA-3-methyladenine%20glycosylase | DNA-3-methyladenine glycosylase also known as 3-alkyladenine DNA glycosylase (AAG) or N-methylpurine DNA glycosylase (MPG) is an enzyme that in humans is encoded by the MPG gene.
Alkyladenine DNA glycosylase is a specific type of DNA glycosylase. This subfamily of monofunctional glycosylases is involved in the recognition of a variety of base lesions, including alkylated and deaminated purines, and initiating their repair via the base excision repair pathway. To date, the human AAG (hAAG) is the only glycosylase identified that excises alkylation-damaged purine bases in human cells.
Function
DNA bases are subject to a large number of anomalies: spontaneous alkylation or oxidative deamination. It is estimated that 104 mutations appear in a typical human cell per day. Albeit it seems to be an insignificant amount considering the extension of the DNA (1010 nucleotides), these mutations lead to changes in the structure and coding potential of the DNA, affecting processes of replication and transcription.
3-Methyladenine DNA glycosilases are able to initiate the base excision repair (BER) of a wide range of substrate bases that, due to their chemical reactivity, suffer inevitable modifications resulting in different biological outcomes. DNA repair mechanisms take on a vital role in maintaining the genomic integrity of cells from different organisms, in particular 3-Methyladenine DNA glycosylases are found in bacteria, yeast, plants, rodents, and humans. Therefore, there are d |
https://en.wikipedia.org/wiki/MLC1 | Membrane protein MLC1 is a protein that in humans is encoded by the MLC1 gene.
MLC1 (also called WKL1) is the only human gene currently associated with megalencephalic leukoencephalopathy with subcortical cysts (MLC). Evidence exists for at least one other gene for MLC, but it has not been mapped or identified.
Function
The function of this gene product is not known; however, homology to other proteins suggests that it may be an integral membrane transport protein. Mutations in this gene have been associated with megalencephalic leukoencephalopathy with subcortical cysts, an autosomal recessive neurological disorder.
The MLC1 protein contains six putative transmembrane domains (S1–S6) and a pore region (P) between S5 and S6. Furthermore, MLC1 has highest homology with the KCNA1 shaker-related voltage-gated potassium channel (Kv1.1). This analysis suggests that MLC1 may be a cation channel.
References
Further reading
External links
GeneReviews/NIH/NCBI/UW entry on Megalencephalic Leukoencephalopathy with Subcortical Cysts |
https://en.wikipedia.org/wiki/SCRIB | SCRIB, also known as Scribble, SCRIBL, or Scribbled homolog (Drosophila), is a scaffold protein which in humans is encoded by the SCRIB gene. It was originally isolated in Drosophila melanogaster in a pathway (also known as the Scribble complex) with DLGAP5 (Discs large) and LLGL1 (Lethal giant larvae) as a tumor suppressor. In humans, SCRIB is found as a membrane protein and is involved in cell migration, cell polarity, and cell proliferation in epithelial cells. There is also strong evidence that SCRIB may play a role in cancer progression because of its strong homology to the Drosophila protein.
Function
In Drosophila melanogaster, SCRIB is involved in synaptic function, neuroblast differentiation, and epithelial polarization. Mechanistically, the human homolog is a scaffold protein linked to cellular differentiation centered on the regulation of epithelial as well as neuronal morphogenesis. Deficiency in SCRIB impairs many aspects of cell polarity and cell movement. SCRIB is also likely involved in establishing apical-basal polarity as well as progression from the G1 phase to S phase in the cell cycle as a result of its relationship with cell proliferation and exocytosis.
The transcribed protein products of the SCRIB gene along with DLGAP5 (Discs large) and LLGL1 (Lethal giant larvae) are components of the Scribble complex that is localized in the basolateral membrane. The Scribble complex plays a role in determining cell polarity and cell proliferation in epithelial |
https://en.wikipedia.org/wiki/Classical%20modal%20logic | In modal logic, a classical modal logic L is any modal logic containing (as axiom or theorem) the duality of the modal operators
that is also closed under the rule
Alternatively, one can give a dual definition of L by which L is classical if and only if it contains (as axiom or theorem)
and is closed under the rule
The weakest classical system is sometimes referred to as E and is non-normal. Both algebraic and neighborhood semantics characterize familiar classical modal systems that are weaker than the weakest normal modal logic K.
Every regular modal logic is classical, and every normal modal logic is regular and hence classical.
References
Chellas, Brian. Modal Logic: An Introduction. Cambridge University Press, 1980.
Modal logic |
https://en.wikipedia.org/wiki/PADI4 | Protein-arginine deiminase type-4, is a human protein which in humans is encoded by the PADI4 gene. The protein as an enzyme, specifically protein-arginine deiminase, a type of hydrolase.
Molecular biology
The human gene is found on the short arm of Chromosome 1 near the telomere (1p36.13). It is located on the Watson (plus) strand and is 55,806 bases long. The protein is 663 amino acids long with a molecular weight of 74,095 Da.
Function
This gene is a member of a gene family which encodes enzymes responsible for the conversion of arginine to citrulline residues (citrullination). This gene may play a role in granulocyte and macrophage development leading to inflammation and immune response. PADI4 plays a role in the epigenetics, the deimination of arginines on histones H3 and H4 can act antagonistically to arginine methylation.
The protein may be found in oligomers and binds 5 calcium ions per subunit. It catalyses the reaction:
Protein L-arginine + H2O = protein L-citrulline + NH3
Subcellular and tissue distribution
It is normally found in the cytoplasm, nucleus and in cytoplasmic granules of eosinophils and neutrophils. It is not expressed in peripheral monocytes or lymphocytes. It is also expressed in rheumatoid arthritis synovial tissues.
References
Further reading |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.