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https://en.wikipedia.org/wiki/KLC1 | Kinesin light chain 1 is a protein that in humans is encoded by the KLC1 gene.
Conventional kinesin is a tetrameric molecule composed of two heavy chains and two light chains, and transports various cargos along microtubules toward their plus ends. The heavy chains provide the motor activity, while the light chains bind to various cargos. This gene encodes a member of the kinesin light chain family. It associates with kinesin heavy chain through an N-terminal domain, and six tetratricopeptide repeat (TPR) motifs are thought to be involved in binding of cargos such as vesicles, mitochondria, and the Golgi complex. Thus, kinesin light chains function as adapter molecules and not motors per se. Although previously named "kinesin 2", this gene is not a member of the kinesin-2 / kinesin heavy chain subfamily of kinesin motor proteins. Extensive alternative splicing produces isoforms with different C-termini that are proposed to bind to different cargos; however, the full-length nature of some of these variants has not been determined.
Interactions
KLC1 has been shown to interact with MAPK8IP3, KIF5B and KIF5A.
References
Further reading |
https://en.wikipedia.org/wiki/Laminin%2C%20beta%202 | Laminin subunit beta-2 is a protein that in humans is encoded by the LAMB2 gene.
Function
Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms, which were formerly designated by Arabic numerals in the order of their discovery, e.g. alpha1beta1gamma1 heterotrimer was known as laminin 1, but the nomenclature now calls for using the numbers of each individual laminin subunit isoform, e.g. what was formerly Laminin 1 is now Laminin 111, and what was formerly Laminin 5 is now Laminin 332. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform |
https://en.wikipedia.org/wiki/Galectin-8 | Galectin-8 is a protein of the galectin family that in humans is encoded by the LGALS8 gene.
Function
This gene encodes a member of the galectin family. Galectins are beta-galactoside-binding animal lectins with conserved carbohydrate recognition domains. The galectins have been implicated in many essential functions including development, differentiation, cell-cell adhesion, cell-matrix interaction, growth regulation, apoptosis, and RNA splicing. This gene is widely expressed in tumoral tissues and seems to be involved in integrin-like cell interactions. Alternatively spliced transcript variants encoding different isoforms have been identified.
Galectin-8, interacts with the mTOR regulatory system composed of SLC38A9, Ragulator, RagAB, RagCD. Galectin-8 controls mTOR causing its inactivation and dissociation from damaged lysosomes, hence transducing the breach of the lysosomal membrane to mTOR. The physiological consequences of mTOR inhibition following lysosomal membrane damage encompass autophagy and metabolic switching.
Role in cellular defence
Galectin-8 has recently been shown to have a role in cellular defence, against both bacterial cytosolic infection and vacuolar damage. Many intracellular bacteria, such as S. enterica serovar Typhimurium and S. flexneri prefer to replicate inside and outside of the vacuole safety respectively, yet these vacuoles may become damaged, exposing bacteria to the host cell cytoplasm. It has been shown that the binding of galectin |
https://en.wikipedia.org/wiki/LIMS1 | LIM and senescent cell antigen-like-containing domain protein 1 is a protein that in humans is encoded by the LIMS1 gene.
Function
The protein encoded by this gene is an adaptor protein which contains five LIM domains, or double zinc fingers. The protein is likely involved in integrin signaling through its LIM domain-mediated interaction with integrin-linked kinase, found in focal adhesion plaques. It is also thought to act as a bridge linking integrin-linked kinase to NCK adaptor protein 2, which is involved in growth factor receptor kinase signaling pathways. Its localization to the periphery of spreading cells also suggests that this protein may play a role in integrin-mediated cell adhesion or spreading.
Interactions
LIMS1 has been shown to interact with Integrin-linked kinase and NCK2.
References
Further reading |
https://en.wikipedia.org/wiki/Loricrin | Loricrin is a protein that in humans is encoded by the LOR gene.
Function
Loricrin is a major protein component of the cornified cell envelope found in terminally differentiated epidermal cells.
Loricrin is expressed in the granular layer of all keratinized epithelial cells of mammals tested including oral, esophageal and stomach mucosa of rodents, tracheal squamous metaplasia of vitamin A deficient hamster and estrogen induced squamous vaginal epithelium of rats.
Clinical significance
Mutations in the LOR gene are associated with Vohwinkel's syndrome and Camisa disease, both inherited skin diseases.
See also
List of cutaneous conditions caused by mutations in keratins
References
Further reading
Structural proteins
Cytoskeleton
Skin |
https://en.wikipedia.org/wiki/Basal%20cell%20adhesion%20molecule | Basal cell adhesion molecule, also known as Lutheran antigen, is a plasma membrane glycoprotein that in humans is encoded by the BCAM gene. BCAM has also recently been designated CD239 (cluster of differentiation 239).
Function
Lutheran blood group glycoprotein is a member of the immunoglobulin superfamily and a receptor for the extracellular matrix protein, laminin. The protein contains five, N-terminus, extracellular immunoglobulin domains, a single transmembrane domain, and a short, C-terminal cytoplasmic tail. This protein may play a role in epithelial cell cancer and in vaso-occlusion of red blood cells in sickle cell disease. Two transcript variants encoding different isoforms have been found for this gene.
Interactions
BCAM has been shown to interact with Laminin, alpha 5. BCAM has also been shown to promote the metastasis of ovarian cancer.
References
Further reading
External links
Clusters of differentiation
Immunoglobulin superfamily
Glycoproteins |
https://en.wikipedia.org/wiki/MAGEA4 | Melanoma-associated antigen 4 is a protein that in humans is encoded by the MAGEA4 gene.
This gene is a member of the MAGEA gene family. The members of this family encode proteins with 50 to 80% sequence identity to each other. The promoters and first exons of the MAGEA genes show considerable variability, suggesting that the existence of this gene family enables the same function to be expressed under different transcriptional controls.
Clinical importance
The MAGEA genes are clustered at chromosomal location Xq28. They have been implicated in some hereditary disorders, such as dyskeratosis congenita. At least four variants encoding the same protein have been found for this gene.
In salivary gland carcinomas, MAGE4 expression correlates to lower-grade histology, lower likelihood of metastases and more favourable survival.
While MAGEA4 is expressed by many tumours, it is almost universally expressed by synovial sarcomas. A targeted treatment to use genetically modified autologous T cells is () undergoing clinical trials.
References
Further reading |
https://en.wikipedia.org/wiki/MAZ%20%28gene%29 | Myc-associated zinc finger protein is a protein that in humans is encoded by the MAZ gene.
Interactions
MAZ (gene) has been shown to interact with BPTF and Deleted in Colorectal Cancer.
References
Further reading |
https://en.wikipedia.org/wiki/ME2%20%28gene%29 | NAD-dependent malic enzyme, mitochondrial is a protein that in humans is encoded by the ME2 gene.
This gene encodes a mitochondrial NAD-dependent malic enzyme, a homotetrameric protein, that catalyzes the oxidative decarboxylation of malate to pyruvate. It had previously been weakly linked to a syndrome known as Friedreich ataxia that has since been shown to be the result of mutation in a completely different gene.
References
Further reading |
https://en.wikipedia.org/wiki/MFGE8 | Milk fat globule-EGF factor 8 protein (Mfge8), also known as lactadherin, is a protein that in humans is encoded by the MFGE8 gene.
Species distribution
Mfge8 is a secreted protein found in vertebrates, including mammals as well as birds.
Function
MFGE8 may function as a cell adhesion protein to connect smooth muscle to elastic fibers in arteries. An amyloid fragment of MFGE8 known as medin accumulates in the aorta with aging. MFGE8 in the vasculature of adults can induce recovery from ischemia by facilitating angiogenesis. It has been suggested that antagonizing MFGE8-induced angiogenesis could be a way of fighting cancer.
MFGE8 contains a phosphatidylserine (PS) binding domain, as well as an arginine-glycine-aspartic acid motif, which enables the binding to integrins. MFGE8 binds PS, which is exposed on the surface of apoptotic cells. Opsonization of the apoptotic cells and binding to integrins on the surface of phagocytic cells, mediates the engulfment of the dead cell.
References
Further reading |
https://en.wikipedia.org/wiki/MST1 | Macrophage-stimulating protein (MSP), also known as hepatocyte growth factor-like protein (HLP, HGFL, or HGFLP), is a protein that in humans is encoded by the MST1 (macrophage-stimulating 1) gene.
References
Further reading |
https://en.wikipedia.org/wiki/MTHFD1 | MTHFD1 is a gene located in humans on chromosome 14 that encodes for a protein with three distinct enzymatic activities. C-1-tetrahydrofolate synthase, cytoplasmic also known as C1-THF synthase is an enzyme that in humans is encoded by the MTHFD1 (methylenetetrahydrofolate dehydrogenase 1) gene.
Function
This gene encodes a protein that possesses three distinct enzymatic activities, methylenetetrahydrofolate dehydrogenase (1.5.1.5), methenyltetrahydrofolate cyclohydrolase (3.5.4.9) and formate–tetrahydrofolate ligase (6.3.4.3). Each of these activities catalyzes one of three sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses. The trifunctional enzymatic activities are conferred by two major domains, an aminoterminal portion containing the dehydrogenase and cyclohydrolase activities and a larger synthetase domain.
Clinical significance
Mutations of the MTHFD1 gene may cause methylenetetrahydrofolate dehydrogenase 1 deficiency, also known as combined immunodeficiency and megaloblastic anemia with or without hyperhomocysteinemia (CIMAH).
References
Further reading
External links
EC 6.3.4 |
https://en.wikipedia.org/wiki/MYH6 | Myosin heavy chain, α isoform (MHC-α) is a protein that in humans is encoded by the MYH6 gene. This isoform is distinct from the ventricular/slow myosin heavy chain isoform, MYH7, referred to as MHC-β. MHC-α isoform is expressed predominantly in human cardiac atria, exhibiting only minor expression in human cardiac ventricles. It is the major protein comprising the cardiac muscle thick filament, and functions in cardiac muscle contraction. Mutations in MYH6 have been associated with late-onset hypertrophic cardiomyopathy, atrial septal defects and sick sinus syndrome.
Structure
MHC-α is a 224 kDa protein composed of 1939 amino acids. The MYH6 gene is located on chromosome 14q12, approximately ~4kb downstream of the MYH7 gene encoding the other major cardiac muscle isoform of myosin heavy chain, MHC-β. MHC-α is a hexameric, asymmetric motor forming the bulk of the thick filament in cardiac muscle; it is the predominant isoform expressed in human cardiac atria, and the lesser expressed isoform (7%) expressed in human cardiac ventricles. MHC-α is composed of N-terminal globular heads (20 nm) that project laterally, and alpha helical tails (130 nm) that dimerize and multimerize into a coiled-coil motif to form the light meromyosin (LMM), thick filament rod. The 9 nm alpha-helical neck region of each MHC-α head non-covalently binds two light chains, atrial essential light chain (MYL4) and atrial regulatory light chain (MYL7). Approximately 300 myosin molecules constitute one t |
https://en.wikipedia.org/wiki/NFE2 |
Transcription factor NF-E2 45 kDa subunit is a protein that in humans is encoded by the NFE2 gene.
It is involved in megakaryocyte production.
Interactions
NFE2 has been shown to interact with CREB-binding protein.
References
Further reading
External links
Transcription factors
Human proteins |
https://en.wikipedia.org/wiki/ATP1A3 | Sodium/potassium-transporting ATPase subunit alpha-3 is an enzyme that in humans is encoded by the ATP1A3 gene.
Function
The protein encoded by this gene belongs to the family of P-type cation transport ATPases, and to the subfamily of Na+/K+-ATPases. Na+/K+-ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The catalytic subunit of Na+/K+-ATPase is encoded by multiple genes. This gene encodes an alpha 3 subunit. ATP1A3 is expressed early in human development, likely underlying pathophysiology related to several ATP1A3 related diseases.
Clinical significance
Disease causing variants of the ATP1A3 gene are known to cause a variety of movement disorders and epilepsies. The known associations include a variety of syndromes, in approximate order of presentation:
Malformation of Cortex Development, including polymicrogyria
Developmental and epileptic encephalopathy 99 (DEE99)
Alternating hemiplegia of childhood (AHC)
Cerebellar ataxia, Areflexia, Pes cavus, Optic atrophy and Sensorineural hearing loss (CAPOS/CAOS syndrome)
Very early-onset schizophrenia
Rapid-onset dys |
https://en.wikipedia.org/wiki/ATP6V0C | V-type proton ATPase 16 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0C gene.
Function
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 and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is part of the V0 domain. This gene had the previous symbols of ATP6C and ATP6L.
References
External links
Further reading |
https://en.wikipedia.org/wiki/NFYC | Nuclear transcription factor Y subunit gamma is a protein that in humans is encoded by the NFYC gene.
Function
The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds with high specificity to CCAAT motifs in the promoter regions in a variety of genes. This gene product, subunit C, forms a tight dimer with the B subunit (NFYB), a prerequisite for subunit A (NFYA) association. The resulting trimer binds to DNA with high specificity and affinity. Subunits B and C each contain a histone-like motif. Observation of the histone nature of these subunits is supported by two types of evidence; protein sequence alignments and experiments with mutants. Additional regulation, preliminarily supported by the EST database, may be represented by alternative splicing in this subunit.
Two microRNAs; miR-30c and miR-30e are located within introns of the nfyc gene. These microRNAs are actively transcribed in human insulin-producing beta cells in the pancreatic islets that also show high expression of nfyc and CDH1 genes. The expression of these intronic microRNAs is essential for maintaining the differentiated phenotype of human islet beta cells. Inhibition of miR-30 family microRNAs induces epithelial-mesenchymal transition of human pancreatic islet cells.
Interactions
NFYC has been shown to interact with Myc.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/NRL%20%28gene%29 | Neural retina-specific leucine zipper protein is a protein that in humans is encoded by the NRL gene.
Function
This gene encodes a basic motif-leucine zipper transcription factor of the Maf subfamily. The encoded protein is conserved among vertebrates and is a critical intrinsic regulator of photoreceptor cell development and function. Mutations in this gene have been associated with retinitis pigmentosa and degenerative diseases of the retina.
See also
Transcription factor
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Retinitis Pigmentosa Overview
Transcription factors |
https://en.wikipedia.org/wiki/PCTK1 | Serine/threonine-protein kinase PCTAIRE-1 is an enzyme that in humans is encoded by the PCTK1 gene.
Function
The protein encoded by this gene belongs to the cdc2/cdkx subfamily of the ser/thr family of protein kinases. It may play a role in signal transduction cascades in terminally differentiated cells. This gene is thought to escape X inactivation. Two transcript variants encoding the same protein have been found for this gene.
Interactions
PCTK1 has been shown to interact with CDK5R1.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/Plakophilin-1 | Plakophilin-1 is a protein that in humans is encoded by the PKP1 gene.
Function
This gene encodes a member of the arm-repeat (armadillo) and plakophilin gene families. Plakophilin proteins contain numerous armadillo repeats, localize to cell desmosomes and nuclei, and participate in linking cadherins to intermediate filaments in the cytoskeleton. This protein may be involved in molecular recruitment and stabilization during desmosome formation. Mutations in this gene have been associated with the ectodermal dysplasia/skin fragility syndrome.
Interactions
PKP1 has been shown to interact with Desmoplakin.
See also
Skin fragility syndrome
References
Further reading
Armadillo-repeat-containing proteins |
https://en.wikipedia.org/wiki/PLAG1 | Zinc finger protein PLAG1 is a protein that in humans is encoded by the PLAG1 gene.
Function
Pleomorphic adenoma gene 1 encodes a zinc finger protein with 2 putative nuclear localization signals. PLAG1, which is developmentally regulated, has been shown to be consistently rearranged in pleomorphic adenomas of the salivary glands. PLAG1 is activated by the reciprocal chromosomal translocations involving 8q12 in a subset of salivary gland pleomorphic adenomas.
Interactions
PLAG1 has been shown to interact with Karyopherin alpha 2.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/SEPT4 | Septin-4 is a protein that in humans is encoded by the SEPT4 gene.
Function
This gene is a member of the septin gene family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse and appear to regulate cytoskeletal organization. The protein encoded by this gene is thought to be part of a complex involved in cytokinesis. 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/PPP2R5B | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform is an enzyme that in humans is encoded by the PPP2R5B gene.
Function
The product of this gene belongs to the phosphatase 2A regulatory subunit B family. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. The B regulatory subunit might modulate substrate selectivity and catalytic activity. This gene encodes a beta isoform of the regulatory subunit B56 subfamily.
Interactions
PPP2R5B has been shown to interact with PPP2R1B and PPP2CA.
References
Further reading |
https://en.wikipedia.org/wiki/PRKAR1B | cAMP-dependent protein kinase type I-beta regulatory subunit is an enzyme that in humans is encoded by the PRKAR1B gene.
Clinical significance
Mutations in PRKAR1B cause neurodegenerative disorder.
Interactions
PRKAR1B has been shown to interact with AKAP1 and PRKAR1A.
References
Further reading
External links
Genes on human chromosome 7 |
https://en.wikipedia.org/wiki/ABCD3 | ATP-binding cassette sub-family D member 3 is a protein that in humans is encoded by the ABCD3 gene.
Function
The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the ALD subfamily, which is involved in peroxisomal import of fatty acids and/or fatty acyl-CoAs in the organelle. All known peroxisomal ABC transporters are half transporters which require a partner half transporter molecule to form a functional homodimeric or heterodimeric transporter. This peroxisomal membrane protein likely plays an important role in peroxisome biogenesis.
Clinical significance
Mutations have been associated with some forms of Zellweger syndrome, a heterogeneous group of peroxisome assembly disorders. However, this association was denied and congenital bile acid synthesis defect-5 (CBAS5) was recently shown to be caused by homozygous mutation in the ABCD3 gene
See also
ATP-binding cassette transporter
Interactions
ABCD3 has been shown to interact with PEX19.
References
Further reading
External links
ABCD3 at The GDB Human Genome Database
ATP-binding cassette transporters |
https://en.wikipedia.org/wiki/RAGE%20%28gene%29 | MAPK/MAK/MRK overlapping kinase is an enzyme that in humans is encoded by the RAGE gene.
References
Further reading |
https://en.wikipedia.org/wiki/PDE11A | Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A is an enzyme that in humans is encoded by the PDE11A gene.
The 3',5'-cyclic nucleotides cAMP and cGMP function as second messengers in a wide variety of signal transduction pathways. 3',5'-cyclic nucleotide phosphodiesterases (PDEs) catalyze the hydrolysis of cAMP and cGMP to the corresponding 5'-monophosphates and provide a mechanism to downregulate cAMP and cGMP signaling. This gene encodes a member of the PDE protein superfamily. Mutations in this gene are a cause of Cushing's disease and adrenocortical hyperplasia. Multiple transcript variants encoding different isoforms have been found for this gene.
Inhibitors
BC11-38
References
Further reading |
https://en.wikipedia.org/wiki/NDUFA13 | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 is an enzyme that in humans is encoded by the NDUFA13 gene. The NDUFA13 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain.
Structure
The NDUFA13 gene is located on the p arm of chromosome 19 in position 13.2 and spans 11,995 base pairs. The gene produces a 17 kDa protein composed of 144 amino acids. NDUFA13 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA13 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I, but it is an accessory subunit that is believed not to be involved in catalysis. The predicted secondary structure is primarily al |
https://en.wikipedia.org/wiki/FZR1 | Fizzy-related protein homolog, also known as hCDH1, is a protein that in humans is encoded by the FZR1 gene.
Interactions
FZR1 has been shown to interact with CDC27 and FBXO5.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Enah/Vasp-like | Ena/VASP-like protein is a member of the Ena/VASP family of proteins that in humans is encoded by the EVL gene.
References
Further reading |
https://en.wikipedia.org/wiki/VPS24 | Charged multivesicular body protein 3 is a protein that in humans is encoded by the VPS24 gene.
Function
This gene encodes a protein that acts in the sorting of transmembrane proteins into lysosomes/vacuoles via the multivesicular body (MVB) pathway. This protein, along with other soluble coiled-coil containing proteins, forms part of the ESCRT-III protein complex that binds to the endosomal membrane and recruits additional cofactors for protein sorting into the MVB. This protein may also co-immunoprecipitate with a member of the IFG-binding protein superfamily. Alternative splicing results in multiple transcript variants encoding different isoforms.
Interactions
VPS24 has been shown to interact with IGFBP7.
References
Further reading |
https://en.wikipedia.org/wiki/RASD1 | Dexamethasone-induced Ras-related protein 1 (RASD1) is a protein that in humans is encoded by the RASD1 gene on chromosome 17. It is ubiquitously expressed in many tissues and cell types. As a member of the Ras superfamily of small G-proteins, RASD1 regulates signal transduction pathways through both G proteins and G protein-coupled receptors. RASD1 has been associated with several cancers. The RASD1 gene also contains one of 27 SNPs associated with increased risk of coronary artery disease.
Structure
Gene
The RASD1 gene resides on chromosome 17 at the band 17p11.2 and contains 2 exons. This gene produces 2 isoforms through alternative splicing. A glucocorticoid response element (GRE) located in the 3'- flanking region of this gene allows glucocorticoids to induce expression of RASD1.
Protein
This protein is a small GTPase belonging to the Ras superfamily. As a Ras superfamily member, RASD1 shares several motifs characteristic of Ras proteins, including four highly conserved GTP binding pocket domains: the phosphate/magnesium binding regions GXXXXGK(S/T) (domain Σ1), DXXG (domain Σ2), and the guanine base binding loops NKXD (domain Σ3) and EXSAK (domain Σ4). These four domains, along with an effector loop, are responsible for binding to other proteins and signaling molecules. Another common Ras motif, the CAAX motif, can be found in the C-terminal of RASD1 and promotes the subcellular localization of RASD1 to the plasma membrane. As a GTPase, RASD1 also shares motifs, su |
https://en.wikipedia.org/wiki/TOLLIP | Toll interacting protein, also known as TOLLIP, is an inhibitory adaptor protein that in humans is encoded by the TOLLIP gene.
Function and regulation
It is an inhibitory adaptor protein within Toll-like receptors (TLR). The TLR pathway is a part of the innate immune system that recognizes structurally conserved molecular patterns of microbial pathogens, leading to an inflammatory immune response.
Tollip interacts with cellular and subcellular membrane compartments such as endosome and lysosome through its C2 domain binding with phosphoinositides. By coordinating organelle communications , Tollip can contribute to the fusion of endo-lysosome and autophagosome. Mice with Tollip deletion exhibit elevated risks for inflammatory diseases such as atherosclerosis and neurodegeneration.
Clinical significance
Polymorphisms in TLR genes have been implicated in various diseases like atopic dermatitis. Recently, variations in the TOLLIP gene have been associated with tuberculosis and idiopathic pulmonary fibrosis.
Interactions
TOLLIP has been shown to interact with TOM1, TLR 2, TLR 4 and IL1RAP.
References
Further reading |
https://en.wikipedia.org/wiki/UGT1A3 | UDP-glucuronosyltransferase 1-3 is an enzyme that in humans is encoded by the UGT1A3 gene.
This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. Substrates of this enzyme include estrone, 2-hydroxyestrone, and metabolites of benzo(a)pyrene.
References
Further reading |
https://en.wikipedia.org/wiki/AHI1 | The Abelson helper integration site 1 (AHI1) is a protein coding gene that is known for the critical role it plays in brain development. Proper cerebellar and cortical development in the human brain depends heavily on AHI1. The AHI1 gene is prominently expressed in the embryonic hindbrain and forebrain. AHI1 specifically encodes the Jouberin protein and mutations in the expression of the gene is known to cause specific forms of Joubert syndrome. Joubert syndrome is autosomal recessive and is characterized by the brain malformations and mental retardation that AHI1 mutations have the potential to induce. AHI1 has also been associated with schizophrenia and autism due to the role it plays in brain development. An AHI1 heterozygous knockout mouse model was studied by Bernard Lerer and his group at Hadassah Medical Center in Jerusalem to elucidate the correlation between alterations in AHI1 expression and the pathogenesis of neuropsychiatric disorders. The core temperatures and corticosterone secretions of the heterozygous knockout mice after exposure to environmental and visceral stress exhibited extreme repression of autonomic nervous system and hypothalamic-pituitary-adrenal responses. The knockout mice demonstrated an increased resilience to different types of stress and these results lead to a correlation between emotional regulation and neuropsychiatric disorders.
Jouberin is a protein that in humans is encoded by the AHI1 gene.
References
External links
Further |
https://en.wikipedia.org/wiki/VPS35 | Vacuolar protein sorting ortholog 35 (VPS35) is a protein involved in autophagy and is implicated in neurodegenerative diseases, such as Parkinson's disease (PD) and Alzheimer's disease (AD). VPS35 is part of a complex called the retromer, which is responsible for transporting select cargo proteins between vesicular structures (e.g., endosomes, lysosomes, vacuoles) and the Golgi apparatus. Mutations in the VPS35 gene (VPS35) cause aberrant autophagy, where cargo proteins fail to be transported and dysfunctional or unnecessary proteins fail to be degraded. There are numerous pathways affected by altered VPS35 levels and activity, which have clinical significance in neurodegeneration. There is therapeutic relevance for VPS35, as interventions aimed at correcting VPS35 function are in speculation.
Gene
In humans, VPS35 is transcribed on chromosome 16q11.2 where is spans about 29.6 kilobases and contains 17 exons. It is evolutionarily conserved and required for survival, as mouse knockout studies have demonstrated embryonic lethality. VPS35 levels peak at postnatal days 10-15 and then decline to a low, stable level throughout adulthood. RNA expression of VPS35 is ubiquitous throughout the body, but are higher in the brain, heart, gonads, spleen, and skeletal muscle, and lower in the lung, liver, kidney, and blood leukocytes.
Protein
VPS35 was first identified in Saccharomyces cerevisiae from a study investigating the formation of lysosome-like vacuoles and sorting of vacuolar |
https://en.wikipedia.org/wiki/ARID1B | AT-rich interactive domain-containing protein 1B is a protein that in humans is encoded by the ARID1B gene. ARID1B is a component of the human SWI/SNF chromatin remodeling complex.
Clinical significance
Germline mutations in ARID1B are associated with Coffin–Siris syndrome. Somatic mutations in ARID1B are associated with several cancer subtypes, suggesting that it is a tumor suppressor gene.
Interactions
ARID1B has been shown to interact with SMARCA4 and SMARCA2.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/TRIB3 | Tribbles homolog 3 is a protein that in humans is encoded by the TRIB3 gene.
Function
The protein encoded by this gene is a putative protein kinase that is induced by the transcription factor NF-kappaB. It is a pseudoenzyme that is thought to be a negative regulator of NF-kappaB, and can also sensitize cells to TNF- and TRAIL-induced apoptosis. In addition, this protein has been reported to negatively regulate the cell survival serine-threonine kinase AKT1. TRIB3 has recently been associated with neuronal signalling, and like TRIB1 and TRIB2, could be considered as a potential allosteric drug target
Interactions
TRIB3 has been shown to interact with:
AKT1,
CSNK2B,
Fibronectin
MCM3AP,
RELA,
SIAH1, and
TIAF1.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/Coherent%20ring | In mathematics, a (left) coherent ring is a ring in which every finitely generated left ideal is finitely presented.
Many theorems about finitely generated modules over Noetherian rings can be extended to finitely presented modules over coherent rings.
Every left Noetherian ring is left coherent. The ring of polynomials in an infinite number of variables over a left Noetherian ring is an example of a left coherent ring that is not left Noetherian.
A ring is left coherent if and only if every direct product of flat right modules is flat , . Compare this to: A ring is left Noetherian if and only if every direct sum of injective left modules is injective.
References
Ring theory |
https://en.wikipedia.org/wiki/ACTG2 | Actin, gamma-enteric smooth muscle is a protein that in humans is encoded by the ACTG2 gene.
Actins are highly conserved proteins that are involved in various types of cell motility, and maintenance of the cytoskeleton. In vertebrates, three main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. Actin, gamma 2, encoded by this gene, is a smooth muscle actin found in enteric tissues.
Interactions
ACTG2 has been shown to interact with Emerin.
References
External links
Further reading
Human proteins |
https://en.wikipedia.org/wiki/HCN2 | Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated ion channel 2 is a protein that in humans is encoded by the HCN2 gene.
Interactions
HCN2 has been shown to interact with HCN1 and HCN4.
Function
The function of the channel is not known although its activation by hyperpolarization alludes to the funny channels in the sinoatrial node of the heart (which form the basis of spontaneous generation of electrical rhythm). These channels have recently been associated with chronic pain and blocking the gene is associated with resolution of neuropathic episodes of pain.
See also
Cyclic nucleotide-gated ion channel
References
Further reading
External links
Ion channels |
https://en.wikipedia.org/wiki/KDM5A | Lysine-specific demethylase 5A is an enzyme that in humans is encoded by the KDM5A gene.
Function
The protein encoded by this gene is a ubiquitously expressed nuclear protein. It binds directly, with several other proteins, to retinoblastoma protein which regulates cell proliferation. It was formerly known as Retinoblastoma Binding Protein 2 (RBP2). This protein also interacts with rhombotin-2 which functions distinctly in erythropoiesis and in T-cell leukemogenesis. Rhombotin-2 is thought to either directly affect the activity of the encoded protein or may indirectly modulate the functions of the retinoblastoma protein by binding to this protein. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
The Drosophila homolog, LID, was found to be an H3K4 histone demethylase that binds to c-Myc. It was recently renamed to Lysine Demethylase 5 (KDM5).
Enzymatically can be designated as a trimethyllysine dioxygenase, which is a member of the alpha-ketoglutarate-dependent hydroxylase superfamily ().
Interactions
JARID1A has been shown to interact with Estrogen receptor alpha, LMO2 and Retinoblastoma protein.
JARID1A is a major component of the circadian clock, the upregulation of which at the end of the sleep phase blocks HDAC1 activity. Blocking HDAC1 activity results in an upregulation of CLOCK and BMAL1 and consequent upregulation of PER proteins. The PSF (polypyrimidine tract-binding protein-associated splicing factor) with |
https://en.wikipedia.org/wiki/RING1 | E3 ubiquitin-protein ligase RING1 is an enzyme that in humans is encoded by the RING1 gene.
Function
This gene belongs to the RING finger family, members of which encode proteins characterized by a RING domain, a zinc-binding motif related to the zinc finger domain. The gene product can bind DNA and can act as a transcriptional repressor. It is associated with the multimeric polycomb group protein complex. The gene product interacts with the polycomb group proteins BMI1, EDR1, and CBX4, and colocalizes with these proteins in large nuclear domains. It interacts with the CBX4 protein via its glycine-rich C-terminal domain. The gene maps to the HLA class II region, where it is contiguous with the RING finger genes FABGL and HKE4.
Interactions
RING1 has been shown to interact with CBX8, BMI1 and RYBP.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/ROBO1 | Roundabout homolog 1 is a protein that in humans is encoded by the ROBO1 gene.
Function
Bilateral symmetric nervous systems have special midline structures that establish a partition between the two mirror image halves. Some axons project toward and across the midline in response to long-range chemoattractants emanating from the midline. The protein encoded by ROBO1 is structurally similar to a Drosophila integral membrane protein which is encoded by the Drosophila roundabout gene (a member of the immunoglobulin gene superfamily) and is both an axon guidance receptor and a cell adhesion receptor, known to be involved in the decision by axons to cross the central nervous system midline. Two transcript variants encoding different isoforms have been found for ROBO1.
Clinical significance
ROBO1 was implicated in a communication disorder based on a Finnish pedigree with severe dyslexia. Analyses revealed a translocation had occurred disrupting ROBO1. Study of the phonological memory component of the language acquisition system suggests that ROBO1 polymorphisms are associated with functioning in this system. The gene is thought to be related to the brain's ability to represent quantities, and is correlated with better math scores of young children in one limited study.
References
Further reading |
https://en.wikipedia.org/wiki/60S%20ribosomal%20protein%20L3 | 60S ribosomal protein L3 is a protein that in humans is encoded by the RPL3 gene.
Function
Ribosomes, the complexes that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. The RPL3 gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L3P family of ribosomal proteins and it is located in the cytoplasm. The protein can bind to the HIV-1 TAR mRNA, and it has been suggested that the protein contributes to tat-mediated transactivation. This gene is co-transcribed with several small nucleolar RNA genes, which are located in several of this gene's introns. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
References
Further reading
Ribosomal proteins |
https://en.wikipedia.org/wiki/60S%20acidic%20ribosomal%20protein%20P1 | 60S acidic ribosomal protein P1 is a protein that in humans is encoded by the RPLP1 gene.
Function
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal phosphoprotein that is a component of the 60S subunit. The protein, which is a functional equivalent of the Escherichia coli L7/L12 ribosomal protein, belongs to the L12P family of ribosomal proteins. It plays an important role in the elongation step of protein synthesis. Unlike most ribosomal proteins, which are basic, the encoded protein is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1 protein can interact with P0 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Two alternatively spliced transcript variants that encode different proteins have been observed. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
Interactions
RPLP1 has been shown to interact with RPLP2.
References
Further reading
External links
Ribosomal proteins |
https://en.wikipedia.org/wiki/40S%20ribosomal%20protein%20S4%2C%20X%20isoform | 40S ribosomal protein S4, X isoform is a protein that in humans is encoded by the RPS4X gene.
Ribosomes, organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes ribosomal protein S4, a component of the 40S subunit. Ribosomal protein S4 is the only ribosomal protein known to be encoded by more than one gene, namely this gene and ribosomal protein S4, Y-linked (RPS4Y). The 2 isoforms encoded by these genes are not identical, but are functionally equivalent. Ribosomal protein S4 belongs to the S4E family of ribosomal proteins. This gene is not subject to X-inactivation. It has been suggested that haploinsufficiency of the ribosomal protein S4 genes plays a role in Turner syndrome; however, this hypothesis is controversial. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
References
Further reading
Ribosomal proteins |
https://en.wikipedia.org/wiki/RPS6KB2 | Ribosomal protein S6 kinase beta-2 is an enzyme that in humans is encoded by the RPS6KB2 gene.
This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains two nonidentical kinase catalytic domains and phosphorylates the S6 ribosomal protein and eucaryotic translation initiation factor 4B (eIF4B). Phosphorylation of S6 leads to an increase in protein synthesis and cell proliferation.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/Coxeter%E2%80%93Todd%20lattice | In mathematics, the Coxeter–Todd lattice K12, discovered by , is a 12-dimensional even integral lattice of discriminant 36 with no norm-2 vectors. It is the sublattice of the Leech lattice fixed by a certain automorphism of order 3, and is analogous to the Barnes–Wall lattice. The automorphism group of the Coxeter–Todd lattice has order 210·37·5·7=78382080, and there are 756 vectors in this lattice of norm 4 (the shortest nonzero vectors in this lattice).
Properties
The Coxeter–Todd lattice can be made into a 6-dimensional lattice self dual over the Eisenstein integers. The automorphism group of this complex lattice has index 2 in the full automorphism group of the Coxeter–Todd lattice and is a complex reflection group (number 34 on the list) with structure 6.PSU4(F3).2, called the Mitchell group.
The genus of the Coxeter–Todd lattice was described by and has 10 isometry classes: all of them other than the Coxeter–Todd lattice have a root system of maximal rank 12.
Construction
Based on Nebe web page we can define K12 using following 6 vectors in 6-dimensional complex coordinates. ω is complex number of order 3 i.e. ω3=1.
(1,0,0,0,0,0), (0,1,0,0,0,0), (0,0,1,0,0,0),
½(1,ω,ω,1,0,0), ½(ω,1,ω,0,1,0), ½(ω,ω,1,0,0,1),
By adding vectors having scalar product -½ and multiplying by ω we can obtain all lattice vectors. We have 15 combinations of two zeros times 16 possible signs gives 240 vectors; plus 6 unit vectors times 2 for signs gives 240+12=252 vectors. Multiply it |
https://en.wikipedia.org/wiki/RTN1 | Reticulon-1 also known as neuroendocrine-specific protein (NSP) is a protein that in humans is encoded by the RTN1 gene.
This gene belongs to the family of reticulon-encoding genes. Reticulons are associated with the endoplasmic reticulum, and are involved in neuroendocrine secretion or in membrane trafficking in neuroendocrine cells. Alternatively spliced transcript variants encoding different isoforms have been identified. Multiple promoters rather than alternative splicing of internal exons seem to be involved in this diversity.
Interactions
RTN1 has been shown to interact with BCL2-like 1 and UGCG.
References
Further reading |
https://en.wikipedia.org/wiki/SALL1 | Sal-like 1 (Drosophila), also known as SALL1, is a protein which in humans is encoded by the SALL1 gene. As the full name suggests, it is one of the human versions of the spalt (sal) gene known in Drosophila.
Function
The protein encoded by this gene is a zinc finger transcriptional repressor and may be part of the NuRD histone deacetylase (HDAC) complex.
Clinical significance
Defects in this gene are a cause of Townes–Brocks syndrome (TBS) as well as branchio-oto-renal syndrome (BOR). Two transcript variants encoding different isoforms have been found for this gene.
Interactions
SALL1 has been shown to interact with TERF1 and UBE2I.
References
External links
GeneReviews/NCBI/NIH/UW entry on Townes-Brocks Syndrome
Further reading
Transcription factors |
https://en.wikipedia.org/wiki/SGCA | Alpha-sarcoglycan is a protein that in humans is encoded by the SGCA gene.
Function
The dystrophin-glycoprotein complex (DGC) comprises a group of proteins that are critical to the stability of muscle fiber membranes and to the linking of the actin cytoskeleton to the extracellular matrix. Components of the DGC include dystrophin (MIM 300377), which is deficient in Duchenne muscular dystrophy (DMD; MIM 310200); syntrophins (e.g., MIM 600026); dystroglycans (MIM 128239); and sarcoglycans, such as adhalin, a 50-kD transmembrane protein (Roberds et al., 1993).[supplied by OMIM]
Interactions
SGCA has been shown to interact with Biglycan.
References
Further reading
External links
LOVD mutation database: SGCA |
https://en.wikipedia.org/wiki/Ileal%20sodium/bile%20acid%20cotransporter | Ileal sodium/bile acid cotransporter, also known as apical sodium–bile acid transporter (ASBT) and ileal bile acid transporter (IBAT), is a bile acid:sodium symporter protein that in humans is encoded by the SLC10A2 gene.
ASBT/IBAT is most highly expressed in the ileum, where it is found on the brush border membrane of enterocytes. It is responsible for the initial uptake of bile acids, particularly conjugated bile acids, from the intestine as part of their enterohepatic circulation.
As a drug target
Several medications to inhibit IBAT are under development. They include elobixibat, under development for the treatment of constipation and irritable bowel syndrome, and volixibat, under development for the treatment of nonalcoholic steatohepatitis.
See also
Solute carrier family
References
Further reading
Solute carrier family |
https://en.wikipedia.org/wiki/STATH | Statherin is a protein in humans that is encoded by the STATH gene. It prevents the precipitation of calcium phosphate in saliva, maintaining a high calcium level in saliva available for remineralisation of tooth enamel and high phosphate levels for buffering.
References
Further reading |
https://en.wikipedia.org/wiki/SULT2B1 | Sulfotransferase family cytosolic 2B member 1 is an enzyme that in humans is encoded by the SULT2B1 gene.
Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic chemical 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 sulfates dehydroepiandrosterone but not 4-nitrophenol, a typical substrate for the phenol and estrogen sulfotransferase subfamilies. Two alternatively spliced variants that encode different isoforms have been described.
See also
Steroid sulfotransferase
Steroidogenic enzyme
References
Further reading |
https://en.wikipedia.org/wiki/SURF1 | Surfeit locus protein 1 (SURF1) is a protein that in humans is encoded by the SURF1 gene. The protein encoded by SURF1 is a component of the mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex (MITRAC complex), which is involved in the regulation of cytochrome c oxidase assembly. Defects in this gene are a cause of Leigh syndrome, a severe neurological disorder that is commonly associated with systemic cytochrome c oxidase (complex IV) deficiency, and Charcot-Marie-Tooth disease 4K (CMT4K).
Structure
SURF1 is located on the q arm of chromosome 9 in position 34.2 and has 9 exons. The SURF1 gene produces a 33.3 kDa protein composed of 300 amino acids. The protein is a member of the SURF1 family, which includes the related yeast protein SHY1 and rickettsial protein RP733. The gene is located in the surfeit gene cluster, a group of very tightly linked genes that do not share sequence similarity, where it shares a bidirectional promoter with SURF2 on the opposite strand. SURF1 is a multi-pass protein that contains two transmembrane regions, one 19 amino acids in length from positions 61-79 and the other 17 amino acids in length from positions 274–290.
Function
This gene encodes a protein localized to the inner mitochondrial membrane and thought to be involved in the biogenesis of the cytochrome c oxidase complex. SURF1 is a multi-pass membrane protein component of the mitochondrial translation regulation assembly intermediate of cytochrom |
https://en.wikipedia.org/wiki/TBX3 | T-box transcription factor TBX3 is a protein that in humans is encoded by the TBX3 gene.
T-box 3 (TBX3) is a member of the T-box gene family of transcription factors which all share a highly conserved DNA binding domain known as the T-box. The T-box gene family consists of 17 members in mouse and humans that are grouped into five subfamilies, namely Brachyury (T), T-brain (Tbr1), TBX1, TBX2, and TBX6. Tbx3 is a member of the Tbx2 subfamily which includes Tbx2, Tbx4 and Tbx5. The human TBX3 gene maps to chromosome 12 at position 12q23-24.1 and consists of 7 exons which encodes a 723 amino acid protein (ENSEMBL assembly release GRCh38.p12).
Transcript splicing
Alternative processing and splicing results in at least 4 distinct TBX3 isoforms with TBX3 and TBX3+2a being the predominant isoforms. TBX3+2a results from alternative splicing of the second intron which leads to the addition of the +2a exon and consequently this isoform has an additional 20 amino acids within the T-box DNA binding domain. The functions of TBX3 and TBX3+2a may vary slightly across different cell types.
Structure and function
TBX3 has domains which are important for its transcription factor function which include a DNA-binding domain (DBD) also called the T-box, a nuclear localization signal, two repression domains (R2 and R1) and an activation domain (A). The T-box recognizes a palindromic DNA sequence (T(G/C)ACACCT AGGTGTGAAATT) known as the T-element, or half sites within this sequence called half |
https://en.wikipedia.org/wiki/CLEC3B | Tetranectin is a protein that in humans is encoded by the CLEC3B gene.
References
External links
Further reading |
https://en.wikipedia.org/wiki/TPD52 | Tumor protein D52 is a protein that in humans is encoded by the TPD52 gene.
Interactions
TPD52 has been shown to interact with TPD52L2, TPD52L1 and MAL2.
References
Further reading |
https://en.wikipedia.org/wiki/Visinin-like%20protein%201 | Visinin-like protein 1 is a protein that in humans is encoded by the VSNL1 gene.
This gene is a member of the visinin/recoverin subfamily of neuronal calcium sensor proteins.
The encoded protein is strongly expressed in granule cells of the cerebellum where it associates with membranes in a calcium-dependent manner and modulates intracellular signaling pathways of the central nervous system by directly or indirectly regulating the activity of adenylyl cyclase. Alternatively spliced transcript variants have been observed, but their full-length nature has not been determined.
References
Further reading
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/CLSPN | Claspin is a protein that in humans is encoded by the CLSPN gene.
Function
Xenopus claspin is an essential upstream regulator of checkpoint kinase 1 and triggers a checkpoint arrest of the cell cycle in the presence of DNA templates in Xenopus egg extracts. The human gene appears to be the homolog Xenopus claspin and its function has not been determined.
Interactions
CLSPN has been shown to interact with:
BRCA1,
CDC45,
CHEK1,
POLE,
RAD17, and
USP7.
References
External links
Further reading |
https://en.wikipedia.org/wiki/MPP5 | MAGUK p55 subfamily member 5 is a protein that in humans is encoded by the MPP5 gene.
Members of the peripheral membrane-associated guanylate kinase (MAGUK) family function in tumor suppression and receptor clustering by forming multiprotein complexes containing distinct sets of transmembrane, cytoskeletal, and cytoplasmic signaling proteins. All MAGUKs contain a PDZ-SH3-GUK core and are divided into 4 subfamilies, DLG-like (see DLG1; MIM 601014), ZO1-like (see TJP1; MIM 601009), p55-like (see MPP1; MIM 305360), and LIN2-like (see CASK; MIM 300172), based on their size and the presence of additional domains (Tseng et al., 2001). MPP5 is a member of the p55-like MAGUK subfamily.[supplied by OMIM]
Interactions
MPP5 has been shown to interact with INADL and FAM71D.
References
Further reading |
https://en.wikipedia.org/wiki/NMNAT1 | Nicotinamide mononucleotide adenylyltransferase 1 (NMNAT1) is an enzyme that in humans is encoded by the nmnat1 gene. It is a member of the nicotinamide-nucleotide adenylyltransferases (NMNATs) which catalyze nicotinamide adenine dinucleotide (NAD) synthesis.
Function
The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca2+ signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD.
NMNAT1 is the most widely expressed of three orthologous genes with nicotinamide-nucleotide adenylyltransferase (NMNAT) activity. Genetically engineered mice lacking NMNAT1 die during early embryogenesis, indicating a critical role of this gene in organismal viability. In contrast, mice lacking NMNAT2, which is expressed predominantly in neural tissues, complete development but die shortly after birth. However, NMNAT1 is dispensable for cell viability, as homozygous deletion of this gene occurs in glioblastoma tumors and cell lines. Other tumors such as osteosarcoma, however, increase the expression of NMNAT1 upon exposure to DNA damaging agents and inactivation of the nmnat1 gene renders these cells more sensitive to chemotherapy with cisplatin. This latter effect involves lowered nuclear NAD levels in N |
https://en.wikipedia.org/wiki/UPF3B | Regulator of nonsense transcripts 3B is a protein that in humans is encoded by the UPF3B gene.
This gene encodes a protein that is part of a post-splicing multiprotein complex involved in both mRNA nuclear export and mRNA surveillance. The encoded protein is one of two functional homologs to yeast Upf3p. 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. It forms with Y14 a complex that binds specifically 20 nt upstream of exon-exon junctions. This gene is located on the long arm of chromosome X. Two splice variants encoding different isoforms have been found for this gene.
Interactions
UPF3B has been shown to interact with UPF2 and UPF1.
References
Further reading |
https://en.wikipedia.org/wiki/Calumenin | Calumenin is a protein that in humans is encoded by the CALU gene.
Calumenin (CALU) is a calcium-binding protein localized in the endoplasmic reticulum (ER) and is involved in such ER functions as protein folding and sorting. Calumenin is a member of the EF-hand superfamily in the ER and Golgi apparatus named CERC. CERC is an acronym for its family members Cab-45, reticulocalbin, Erc-55 (RCN2), and calumenin. The CALU gene encodes a deduced 315-amino acid protein containing 6 EF-hand motifs, 1 potential N-glycosylation site, and a C-terminal ER retention signal. The human and mouse CALU proteins are 98% identical. CALU mRNA is ubiquitously expressed in human tissues and maps to 7q32.
References
External links
Further reading
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/CBR1 | Carbonyl reductase 1, also known as CBR1, is an enzyme which in humans is encoded by the CBR1 gene. The protein encoded by this gene belongs to the short-chain dehydrogenases/reductases (SDR) family, which function as NADPH-dependent oxidoreductases having wide specificity for carbonyl compounds, such as quinones, prostaglandins, and various xenobiotics. Alternatively spliced transcript variants have been found for this gene.
Function
Carbonyl reductase is one of several monomeric, NADPH-dependent oxidoreductases having wide specificity for carbonyl compounds. This enzyme is widely distributed in human tissues. Another carbonyl reductase gene, CBR3, lies close to this gene on chromosome 21q22.12. CBR1 metabolizes many toxic environmental quinones and pharmacological relevant substrates such as the anticancer doxorubicin. Several studies have shown that CBR1 plays a protective role in oxidative stress, neurodegeneration, and apoptosis. In addition, CBR1 inactivates lipid aldehydes during oxidative stress in cells. Therefore, CBR1 may play a beneficial role in protecting against cellular damage resulting from oxidative stress.
Polymorphisms
Up-to-date two non-synonymous polymorphisms on CBR1 have been identified. The CBR1 V88I polymorphism encodes for a valine-to-isoleucine substitution at position 88 of the aminoacid chain. In vitro studies with recombinant proteins indicate that the CBR1 V88 isoform has a higher Vmax towards the substrates menadione (vitamin K3) and dau |
https://en.wikipedia.org/wiki/LAT2 | Linker for activation of T-cells family member 2 is a protein that in humans is encoded by the LAT2 gene.
This gene is one of the contiguous genes at 7q11.23 commonly deleted in Williams syndrome, a multisystem developmental disorder. This gene consists of at least 14 exons, and its alternative splicing generates 3 transcript variants, all encoding the same protein.
References
Further reading |
https://en.wikipedia.org/wiki/WHSC2 | Negative elongation factor A is a protein that in humans is encoded by the WHSC2 gene.
Function
This gene is expressed ubiquitously with higher levels in fetal than in adult tissues. It encodes a protein sharing 93% sequence identity with the mouse protein. Wolf-Hirschhorn syndrome (WHS) is a malformation syndrome associated with a hemizygous deletion of the distal short arm of chromosome 4. This gene is mapped to the 165 kb WHS critical region, and may play a role in the phenotype of the WHS or Pitt-Rogers-Danks syndrome. The encoded protein is found to be capable of reacting with HLA-A2-restricted and tumor-specific cytotoxic T lymphocytes, suggesting a target for use in specific immunotherapy for a large number of cancer patients. This protein has also been shown to be a member of the NELF (negative elongation factor) protein complex that participates in the regulation of RNA polymerase II transcription elongation. WHSC2 encodes the NELF-A subunit of the NELF complex.
Interactions
WHSC2 has been shown to interact with RDBP.
References
Further reading |
https://en.wikipedia.org/wiki/PTP4A1 | Protein tyrosine phosphatase type IVA 1 is an enzyme that in humans is encoded by the PTP4A1 gene.
The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs), which contains a PTP domain and a characteristic C-terminal prenylation motif. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This tyrosine phosphatase is a nuclear protein, but may primarily associate with plasma membrane. The surface membrane association of this protein depends on its C-terminal prenylation. Overexpression of this gene in mammalian cells conferred a transformed phenotype, which implicated its role in the tumorigenesis. Studies in rat suggested that this gene may be an immediate-early gene in mitogen-stimulated cells.
Interactions
PTP4A1 has been shown to interact with ATF7.
References
Further reading |
https://en.wikipedia.org/wiki/CSDE1 | Cold shock domain-containing protein E1 is a protein that in humans is encoded by the CSDE1 gene.
References
External links
Further reading |
https://en.wikipedia.org/wiki/DAP3 | 28S ribosomal protein S29, mitochondrial, also known as death-associated protein 3 (DAP3), is a protein that in humans is encoded by the DAP3 gene on chromosome 1. This gene encodes a 28S subunit protein of the mitochondrial ribosome (mitoribosome) and plays key roles in translation, cellular respiration, and apoptosis. Moreover, DAP3 is associated with cancer development, but has been observed to aid some cancers while suppressing others.
Structure
The DAP3 gene encodes a 46 kDa protein located in the lower area of the small mitoribosomal subunit. This protein contains a P-loop motif that binds GTP and a highly conserved 17-residue targeting sequence responsible for its localization to the mitochondria. Of interest, many of the phosphorylation sites on this protein are highly conserved and clustered around GTP-binding motifs.
Several splice variants were observed in human ESTs that differ largely in the 5’ UTR region. Pseudogenes for this gene are also found in chromosomes 1 and 2.
Function
DAP3 is a 28S subunit protein of mitoribosomes and localizes to the mitochondrial matrix. As part of the mitoribosome, DAP3 participates in the translation of the 13 ETC complex proteins encoded in the mitochondrial genome, and consequently, in the regulation of cellular respiration. As a member of the death-associated protein (DAP) family, DAP3 can also be found outside of the mitochondria to initiate the extrinsic apoptotic pathway through its interactions with apoptotic factors, s |
https://en.wikipedia.org/wiki/Melanoma%20inhibitory%20activity | Melanoma-derived growth regulatory protein is a protein that in humans is encoded by the MIA gene.
It is a marker for malignant melanoma.
References
Further reading
Human proteins |
https://en.wikipedia.org/wiki/DNA%20repair%20and%20recombination%20protein%20RAD54-like | DNA repair and recombination protein RAD54-like is a protein that in humans is encoded by the RAD54L gene.
The protein encoded by this gene belongs to the DEAD-like helicase superfamily, and shares similarity with Saccharomyces cerevisiae Rad54, a protein known to be involved in the homologous recombination and repair of DNA. This protein has been shown to play a role in homologous recombination related repair of DNA double-strand breaks. The binding of this protein to double-strand DNA induces a DNA topological change, which is thought to facilitate homologous DNA pairing, and stimulate DNA recombination.
RAD54 is one of the key proteins necessary for homologous recombination and DNA repair in many organisms. Without functional RAD54, tumor development is more likely. RAD54 was initially described in the budding yeast Saccharomyces cerevisiae as being a member of the evolutionarily conserved RAD52 epistasis group, which additionally includes RAD51, RAD52, RAD55, and RAD57 factors. This group is believed to be involved in DNA recombination events and repair mechanisms, especially those involving double-stranded DNA breaks during both mitosis and meiosis. Recently a human homologue of the yeast RAD54 was discovered and termed hRAD54.
Human gene
Human RAD54, or hRAD54, is linked to chromosome 1p32. It encodes a protein, composed of 747 amino acids, that is 52% identical to its yeast counterpart. These two proteins also share many functional similarities. The RAD54 encoded p |
https://en.wikipedia.org/wiki/Plakophilin-4 | Plakophilin-4 is a protein that in humans is encoded by the PKP4 gene.
Function
Armadillo-like proteins are characterized by a series of armadillo repeats, first defined in the Drosophila 'armadillo' gene product, that are typically 42 to 45 amino acids in length. These proteins can be divided into subfamilies based on their number of repeats, their overall sequence similarity, and the dispersion of the repeats throughout their sequences. Members of the p120(ctn)/plakophilin subfamily of Armadillo-like proteins, including CTNND1, CTNND2, PKP1, PKP2, PKP4, and ARVCF. PKP4 may be a component of desmosomal plaque and other adhesion plaques and is thought to be involved in regulating junctional plaque organization and cadherin function. Multiple transcript variants have been found for this gene, but the full-length nature of only two of them have been described so far. These two variants encode distinct isoforms.
Interactions
PKP4 has been shown to interact with:
Erbin,
PDZD2, and
PSEN1.
References
Further reading
Armadillo-repeat-containing proteins |
https://en.wikipedia.org/wiki/BHLHB2 | Class E basic helix-loop-helix protein 40 is a protein that in humans is encoded by the BHLHE40 gene.
Function
DEC1 encodes a basic helix-loop-helix protein expressed in various tissues. Expression in the chondrocytes is responsive to the addition of Bt2cAMP. Differentiated embryo chondrocyte expressed gene 1 is believed to be involved in the control of cell differentiation.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/VAPB | Vesicle-associated membrane protein-associated protein B/C is a protein that in humans is encoded by the VAPB gene. The VAPB gene is found on the 20th human chromosome. Together with VAPA, it forms the VAP protein family.
Function
The protein encoded by this gene is a type IV membrane protein found in plasma and intracellular vesicle membranes. The encoded protein is found as a homodimer and as a heterodimer with VAPA. This protein also can interact with VAMP1 and VAMP2 and may be involved in vesicle trafficking.
Like VAPA, VAPB binds to proteins that contain a FFAT motif. Considerable interest in VAPB has arisen because mutations in this protein are associated with rare, familial forms of motor neuron disease (also called amyotrophic lateral sclerosis and Lou Gehrig's disease).
References
Further reading |
https://en.wikipedia.org/wiki/RAB9A | Ras-related protein Rab-9A is a protein that in humans is encoded by the RAB9A gene.
Interactions
RAB9A has been shown to interact with RABEPK, TIP47 and the Biogenesis of lysosome-related organelles complex 3.
References
Further reading |
https://en.wikipedia.org/wiki/MYOT | Myotilin is a protein that in humans is encoded by the MYOT gene. Myotilin (myofibrillar titin-like protein) also known as TTID (TiTin Immunoglobulin Domain) is a muscle protein that is found within the Z-disc of sarcomeres.
Structure
Myotilin is a 55.3 kDa protein composed of 496 amino acids. Myotilin was originally identified as a novel alpha-actinin binding partner with two Ig-like domains, that localized to the Z-disc. The I-type Ig-like domains reside at the C-terminal half, and are most homologous to Ig domains 2-3 of palladin and Ig domains 4-5 of myopalladin and more distantly related to Z-disc Ig domains 7 and 8 of titin. The C-terminal region hosts the binding sites for Z-band proteins, and 2 Ig domains are the site of homodimerization for myotilin. By contrast, the N-terminal part of myotilin is unique, consisting of a serine-rich region with no homology to known proteins. Several disease-associated mutations involve serine residues within the serine-rich domain. Myotilin expression in human tissues is mainly restricted to striated muscles and nerves. In muscles, myotilin is predominantly found within the Z-discs. Myotilin forms homodimers and binds alpha-actinin, actin, Filamin C, FATZ-1, FATZ-2 and ZASP.
Function
Myotilin is a structural protein that, along with titin and alpha-actinin give structural integrity to sarcomeres at Z-discs in striated muscle. Myotilin induces the formation of actin bundles in vitro and in non-muscle cells. A ternary complex myotil |
https://en.wikipedia.org/wiki/LITAF | Lipopolysaccharide-induced tumor necrosis factor-alpha factor is a protein that in humans is encoded by the LITAF gene.
It is associated with Charcot–Marie–Tooth disease 1C.
References
External links
GeneReviews/NCBI/NIH/UW entry on Charcot-Marie-Tooth Neuropathy Type 1
Further reading |
https://en.wikipedia.org/wiki/DLGAP5 | Disks large-associated protein 5 (DAP-5) also known as discs large homolog 7 (DLG7) or hepatoma up-regulated protein (HURP) is a protein that in humans is encoded by the DLGAP5 gene.
DLG7 is a kinetochore protein that stabilizes microtubules in vicinity of chromosomes. DLG7 controls spindle dynamics, promotes interkinetochore tension and efficient kinetochore capture. DGL7 is a part of Ran-dependent complex. Stabilization of DGL7 in cell occurs due to phosphorylation by Aurora A kinase. Expression of DGL7 is found in cancer and stem cells.
References
Further reading
External links |
https://en.wikipedia.org/wiki/ARHGEF11 | Rho guanine nucleotide exchange factor 11 is a protein that in humans is encoded by the ARHGEF11 gene. This protein is also called RhoGEF11 or PDZ-RhoGEF.
Function
Rho guanine nucleotide exchange factor 11 is guanine nucleotide exchange factor (GEF) for the RhoA small GTPase protein. Rho is a small GTPase protein that is inactive when bound to the guanine nucleotide GDP. But when acted on by Rho GEF proteins such as RhoGEF1, this GDP is released and replaced by GTP, leading to the active state of Rho. In this active, GTP-bound conformation, Rho can bind to and activate specific effector proteins and enzymes to regulate cellular functions. In particular, active Rho is a major regulator of the cell actin cytoskeleton.
RhoGEF11 is a member of a group of four RhoGEF proteins known to be activated by G protein coupled receptors coupled to the G12 and G13 heterotrimeric G proteins. The others are ARHGEF1 (also known as p115-RhoGEF), ARHGEF12 (also known as LARG) and AKAP13 (also known as ARHGEF13 and Lbc). GPCR-regulated RhoGEF11 (and these related GEF proteins) acts as an effector for G12 and G13 G proteins. In addition to being activated by G12 or G13 G proteins, three of these four RhoGEF proteins (ARHGEF1/11/12) also function as RGS family GTPase-activating proteins (GAPs) to increase the rate of GTP hydrolysis of G12/G13 alpha proteins (which are themselves GTPase proteins). This action increases the rate of G protein deactivation, limiting the time during which these Rho |
https://en.wikipedia.org/wiki/TLK1 | Serine/threonine-protein kinase tousled-like 1 is an enzyme that in humans is encoded by the TLK1 gene.
Function
The Tousled-like kinases, first described in Arabidopsis, are nuclear serine/threonine kinases that are potentially involved in the regulation of chromatin assembly.[supplied by OMIM]
Interactions
TLK1 has been shown to interact with ASF1B, ASF1A and TLK2.
References
Further reading |
https://en.wikipedia.org/wiki/MED6 | Mediator of RNA polymerase II transcription subunit 6 is one of the subunits of the Mediator complex. It is an enzyme that in humans is encoded by the MED6 gene.
Protein family
This family of proteins represent the transcriptional mediator protein subunit 6 that is required for activation of many RNA polymerase II promoters and which are conserved from yeast to humans.
Interactions
MED6 has been shown to interact with:
Cyclin-dependent kinase 8,
Estrogen receptor alpha,
MED21, and
Thyroid hormone receptor alpha.
References
Further reading
External links
Protein families |
https://en.wikipedia.org/wiki/BIRC7 | Baculoviral IAP repeat-containing protein 7 is a protein that in humans is encoded by the BIRC7 gene.
The protein encoded by this gene is a member of the family of inhibitor of apoptosis proteins (IAP) and contains a single copy of a baculovirus IAP repeat (BIR) as well as a RING-type zinc finger domain. The BIR domain is essential for inhibitory activity and interacts with caspases, while the RING finger domain sometimes enhances antiapoptotic activity but does not inhibit apoptosis alone. Two transcript variants encoding different isoforms have been found for this gene. The two isoforms have different antiapoptotic properties, with isoform alpha protecting cells from apoptosis induced by staurosporine and isoform b protecting cells from apoptosis induced by etoposide.
In melanoma, BIRC7 gene expression is regulated by the Microphthalmia-associated transcription factor.
References
External links
Further reading |
https://en.wikipedia.org/wiki/MAP1LC3B | Microtubule-associated proteins 1A/1B light chain 3B (hereafter referred to as LC3) is a protein that in humans is encoded by the MAP1LC3B gene. LC3 is a central protein in the autophagy pathway where it functions in autophagy substrate selection and autophagosome biogenesis. LC3 is the most widely used marker of autophagosomes.
Discovery
LC3 was originally identified as a microtubule associated protein in rat brain. However it was later found that the primary function of LC3 is in autophagy, a process that involves the bulk degradation of cytoplasmic components.
The ATG8 protein family
MAP1LC3B is a member of the highly conserved ATG8 protein family. ATG8 proteins are present in all known eukaryotic organisms. The animal ATG8 family comprises three subfamilies: (i) microtubule-associated protein 1 light chain 3 (MAP1LC3); (ii) Golgi-associated ATPase enhancer of 16 kDa (GATE-16); and (iii) γ-amino-butyric acid receptor-associate protein (GABARAP). MAP1LC3B is one of the four genes in the MAP1LC3 subfamily (others include MAP1LC3A, MAP1LC3C, and MAP1LC3B2).
Function
Cytoplasmic LC3
Newly synthesized LC3's C-terminus is hydrolyzed by a cysteine protease called ATG4B exposing Gly120, termed LC3-I. LC3-I, through a series of ubiquitin-like reactions involving enzymes ATG7, ATG3, and ATG12-ATG5-ATG16, becomes conjugated to the head group of the lipid phosphatidylethanolamine. The lipid modified form of LC3, referred to as LC3-II, is believed to be involved in autophagos |
https://en.wikipedia.org/wiki/BRIP1 | Fanconi anemia group J protein is a protein that in humans is encoded by the BRCA1-interacting protein 1 (BRIP1) gene.
Function
The protein encoded by this gene is a member of the RecQ DEAH helicase family and interacts with the BRCT repeats of breast cancer, type 1 (BRCA1). The bound complex is important in the normal double-strand break repair function of breast cancer, type 1 (BRCA1). This gene may be a target of germline cancer-inducing mutations.
This protein also appears to be important in ovarian cancer where it seems to act as a tumor suppressor. Mutations in BRIP1 are associated with a 10-15% risk of ovarian cancer.
BRIP1 appears to have an important role in neuronal cells by suppressing oxidative stress, excitotoxicity induced DNA damage, and in protecting the integrity of mitochondria. A deficiency of BRIP1 causes increased DNA damage, mitochondrial abnormalities and neuronal cell death.
DNA repair
BRIP1 protein is a DNA helicase that is employed in homologous recombinational repair, and in the response of the cell to DNA replication stress. In part, BRIP1 carries out its function through interaction with other key DNA repair proteins, specifically MLH1, BRCA1 and BLM. This group of proteins helps to ensuring genome stability, and in particular repairs DNA double-strand breaks during prophase 1 of meiosis.
Interactions
BRIP1 has been shown to interact with BRCA1.
References
Further reading
External links
External links
Human proteins |
https://en.wikipedia.org/wiki/CARD11 | Caspase recruitment domain-containing protein 11 also known as CARD-containing MAGUK protein 1 (Carma 1) is a protein in the CARD-CC protein family that in humans is encoded by the CARD11 gene. CARD 11 is a membrane associated protein that is found in various human tissues, including the thymus, spleen, liver, and peripheral blood leukocytes. Similarly, CARD 11 is also found in abundance in various lines of cancer cells.
Function
The protein encoded by this gene belongs to the membrane-associated guanylate kinase (MAGUK) family, a class of proteins that functions as molecular scaffolds for the assembly of multiprotein complexes at specialized regions of the plasma membrane. This protein is also a member of the CARD protein family, which is defined by carrying a characteristic caspase-associated recruitment domain (CARD). CARD11 (CARMA1) has a domain structure similar to that of CARD10 (CARMA3) and CARD14 (CARMA2) as a member of the CARD-CC family with a C terminal MAGUK domain (the so-called CARMA proteins). The CARD domain of proteins in the CARD-CC family have been shown to specifically interact with BCL10, a protein known to function as a positive regulator of NF-κB activation by recruitment and activation of MALT1. When overexpressed in cells, this protein family activates NF-κB and induces the phosphorylation of BCL10.
CARD11 is critical for T cell and B cell function and is activated after T cell receptor or B cell receptor stimulation. After receptor stimulation, C |
https://en.wikipedia.org/wiki/MAP1LC3A | Microtubule-associated proteins 1A/1B light chain 3A is a protein that in humans is encoded by the MAP1LC3A gene. Two transcript variants encoding different isoforms have been found for this gene.
Function
MAP1A and MAP1B are microtubule-associated proteins which mediate the physical interactions between microtubules and components of the cytoskeleton. MAP1A and MAP1B each consist of a heavy chain subunit and multiple light chain subunits. The protein encoded by this gene is one of the light chain subunits and can associate with either MAP1A or MAP1B.
MAPLC3A is one of the mammalian homologues of yeast ATG8, an important marker and effector of autophagy.
Regulation
MAP1LC3A is regulated by several post-translational modifications. These include covalent linkage of the C-terminus to phosphatidylethanolamine in autophagic membranes, and phosphorylation by protein kinase A, which downregulates its autophagy functions. Noncovalent interactions are important for its cargo targeting functions in selective autophagy. For example, it has been shown to interact with sequestosome 1.
References
Further reading |
https://en.wikipedia.org/wiki/MotherRock | MotherRock was an energy sector hedge fund, one of the biggest traders of natural gas derivatives in New York, with assets of around $430 million at one point. It closed in August 2006 due losing money on its bets that natural gas prices would fall. In 2006 the summer heat led to prices increasing and in June 2006 MotherRock Energy Fund lost 24.6 percent and then in July 25.5 percent. Leveraged positions exacerbated the situation and eventually led to a loss of around $230 million in June and July 2006.
History
The fund was started by J. Robert Collins, with Conrad Goerl and ex-NYMEX vice president John D'Agostino in early 2005.
Senate findings
When investigating sudden price movements in the natural gas markets, and specifically the role Amaranth Advisors played in these movements, it was ascertained that Amaranth's aggressive trading was the only reason for MotherRock's collapse.
It was found that Amaranth could distort market prices through large trades. On July 31, 2006, Amaranth's trading caused a 72% jump in the price spread that directly affected MotherRock's positions so badly that the latter could not meet its margin calls. MotherRock folded soon afterwards.
References
Defunct hedge funds
Defunct financial services companies of the United States
Financial services companies established in 2005
Financial services companies disestablished in 2006 |
https://en.wikipedia.org/wiki/Body%20schema | Body schema is a concept used in several disciplines, including psychology, neuroscience, philosophy, sports medicine, and robotics. The neurologist Sir Henry Head originally defined it as a postural model of the body that actively organizes and modifies 'the impressions produced by incoming sensory impulses in such a way that the final sensation of body position, or of locality, rises into consciousness charged with a relation to something that has happened before'. As a postural model that keeps track of limb position, it plays an important role in control of action. It involves aspects of both central (brain processes) and peripheral (sensory, proprioceptive) systems. Thus, a body schema can be considered the collection of processes that registers the posture of one's body parts in space. The schema is updated during body movement. This is typically a non-conscious process, and is used primarily for spatial organization of action. It is therefore a pragmatic representation of the body’s spatial properties, which includes the length of limbs and limb segments, their arrangement, the configuration of the segments in space, and the shape of the body surface. Body schema also plays an important role in the integration and use of tools by humans.
A clear differentiation of body schema from body image has developed gradually.
History
Henry Head, an English neurologist who conducted pioneering work into the somatosensory system and sensory nerves, together with British neurol |
https://en.wikipedia.org/wiki/Medial%20giant%20interneuron | The medial giant interneuron (MG) is an interneuron in the abdominal nerve cord of crayfish. It is part of the system that controls the caridoid escape reaction of crayfish, clawed lobsters, and other decapod crustaceans. Crayfish have a pair of medial giants running the length of the entire animal, and are the largest neurons in the animal.
When a crayfish is given a sudden visual or tactile stimulus to the front part of the animal, the MG activates fast flexor motor neurons that cause the abdomen to flex, resulting in the crayfish moving directly backward, away from the source of the stimulation. This connection was first demonstrated by C. A. G. Wiersma in the red swamp crayfish, Procambarus clarkii.
The medial giant interneurons are less well studied than the lateral giant neurons, which trigger a similar escape behavior.
See also
Squid giant axon
References
Neurons
Crayfish |
https://en.wikipedia.org/wiki/David%20Aldous | David John Aldous FRS (born 13 July 1952) is a mathematician known for his research on probability theory and its applications, in particular in topics such as exchangeability, weak convergence, Markov chain mixing times, the continuum random tree and stochastic coalescence. He entered St. John's College, Cambridge, in 1970 and received his Ph.D. at the University of Cambridge in 1977 under his advisor, D. J. H. Garling. Aldous was on the faculty at University of California, Berkeley from 1979 until his retirement in 2018.
He was awarded the Rollo Davidson Prize in 1980, the Loève Prize in 1993, and was elected a Fellow of the Royal Society in 1994. In 2004, Aldous was elected a Fellow of the American Academy of Arts and Sciences. From 2004 to 2010, Aldous was an Andrew Dickson White Professor-at-Large at Cornell University. He was an invited speaker at the International Congress of Mathematicians (ICM) in 1998 in Berlin and a plenary speaker at the ICM in 2010 in Hyderabad. In 2012 he became a fellow of the American Mathematical Society. He discovered (independently from Andrei Broder) an algorithm for generating a uniform spanning tree of a given graph.
Selected publications
Books
As editor
(pbk reprint of 1995 original)
(pbk reprint of 1996 original)
Papers
Aldous, David, "Deterministic and stochastic models for coalescence (aggregation and coagulation): a review of the mean-field theory for probabilists". Bernoulli 5 (1999) pp. 3–48.
Aldous, David, "Exchangeabilit |
https://en.wikipedia.org/wiki/Plane%20Dumb | Plane Dumb is the 12th Van Beuren Tom and Jerry cartoon, released on June 4, 1932. The cartoon's soundtrack is done by Gene Rodemich.
Plot
Tom and Jerry are flying a small airplane and find themselves off the coast of Africa. In an ill-advised effort to fit in among the natives, the two decide to don blackface and talk in a stereotypical African-American dialect. While doing this, the plane goes off balance and crashes into the ocean. After encounters with sharks, an overly-friendly octopus, and a whale, Tom and Jerry make it to the mainland. They are confronted by beasts of the African jungle, from which they take refuge in a cave, where they meet some skeletal Africans that were retooled from the first Tom and Jerry short, "Wot a Night." Once Tom and Jerry come out of the cave, African tribesmen (also stereotypically portrayed as spear-chuckers with bones in their hair) appear from behind almost every rock and crevice, outraged at the sight of the two in blackface, and begin an angry pursuit. The cartoon ends with Tom and Jerry wiping the blackface off their face, still running away from the Africans.
External links
Tom and Jerry (Van Beuren)
American animated short films
Blackface minstrel shows and films
Film controversies
African-American-related controversies in film
Race-related controversies in animation
Race-related controversies in film
1932 short films
1930s English-language films
1930s buddy comedy films
American buddy comedy films
Films set in Africa
RKO P |
https://en.wikipedia.org/wiki/Tubular%20fluid | Tubular fluid is the fluid in the tubules of the kidney. It starts as a renal ultrafiltrate in the glomerulus, changes composition through the nephron, and ends up as urine leaving through the ureters.
Composition table
The composition of tubular fluid changes throughout the nephron, from the proximal tubule to the collecting duct and then as it exits the body, from the ureter.
References
Kidney
Urology |
https://en.wikipedia.org/wiki/Pencran | Pencran (; ) is a commune in the Finistère department of Brittany in north-western France.
Geography
Climate
Pencran has a oceanic climate (Köppen climate classification Cfb). The average annual temperature in Pencran is . The average annual rainfall is with December as the wettest month. The temperatures are highest on average in August, at around , and lowest in January, at around . The highest temperature ever recorded in Pencran was on 9 August 2003; the coldest temperature ever recorded was on 2 January 1997.
Population
Inhabitants of Pencran are called in French Pencranais.
Notable Pencranais
Paul Le Guen, former football player and former Rangers F.C manager
See also
Communes of the Finistère department
Pencran Parish close
References
External links
Official website
Mayors of Finistère Association
Communes of Finistère |
https://en.wikipedia.org/wiki/Pleyber-Christ | Pleyber-Christ (; ) is a commune in the Finistère department of Brittany in north-western France.
Geography
Climate
Pleyber-Christ has a oceanic climate (Köppen climate classification Cfb). The average annual temperature in Pleyber-Christ is . The average annual rainfall is with December as the wettest month. The temperatures are highest on average in August, at around , and lowest in January, at around . The highest temperature ever recorded in Pleyber-Christ was on 9 August 2003; the coldest temperature ever recorded was on 2 January 1997.
Population
Inhabitants of Pleyber-Christ are called in French Pleybériens.
Breton language
In 2008, 7.05% of primary-school children attended bilingual schools, where Breton language is taught alongside French.[1]
Twinning
Pleyber-Christ was twinned with Lostwithiel in Cornwall, UK in 1979. The people in the Twinning Associations of both towns usually meet up every year, alternating between Lostwithiel and Pleyber-Christ.
See also
Communes of the Finistère department
Roland Doré sculptor
Pleyber-Christ Parish close
References
External links
Mayors of Finistère Association
Communes of Finistère |
https://en.wikipedia.org/wiki/Kazuhiko%20Chiba | is a Japanese footballer. He currently plays for the J2 League club Albirex Niigata.
Club statistics
Updated to 5 May 2021.
1Includes Japanese Super Cup, FIFA Club World Cup and J. League Championship.
National team statistics
Honours
Club
Sanfrecce Hiroshima
J1 League: 2012, 2013, 2015
Japanese Super Cup: 2013, 2014, 2016
International
Japan
EAFF East Asian Cup: 2013
References
External links
Japan National Football Team Database
Profile at Sanfrecce Hiroshima
Profile at Albirex Niigata
1985 births
Living people
Association football people from Hokkaido
Japanese men's footballers
Japan men's international footballers
Eerste Divisie players
J1 League players
J2 League players
AGOVV players
FC Dordrecht players
Albirex Niigata players
Sanfrecce Hiroshima players
Nagoya Grampus players
Japanese expatriate men's footballers
Expatriate men's footballers in the Netherlands
Japanese expatriate sportspeople in the Netherlands
Men's association football defenders
People from Kushiro, Hokkaido |
https://en.wikipedia.org/wiki/Linn%20Nyr%C3%B8nning | Linn Nyrønning (born 4 June 1981) is a Norwegian football midfielder who currently plays for Trondheims-Ørn.
References
Profile at club site
National team statistics
1981 births
Living people
Norwegian women's footballers
Norway women's international footballers
SK Trondheims-Ørn players
Women's association football midfielders |
https://en.wikipedia.org/wiki/Rik%20Van%20Linden | Rik Van Linden (born 28 July 1949 in Wilrijk, Antwerp) is a Belgian former road bicycle racer. He won the points classification in the 1975 Tour de France, ahead of Eddy Merckx.
Van Linden also won several stages in all of the three Grand Tours, and the classic cycle race Paris–Tours twice (1971, 1973).
Through his career, he eventually won 359 races, of which 73 as junior cyclist in 1968.
Major results
Road
1968
1st Road race, National Junior Road Championships
1969
1st Ronde van Vlaanderen Beloften
1970
1st Omnium, National Amateur Track Championships
1971
1st Paris–Tours
2nd Kampioenschap van Vlaanderen
2nd Omloop der Zennevallei
3rd GP di Larciano
8th Trofeo Matteotti
9th Scheldeprijs
1972
Tour de France
1st Stage 2
2nd Points Classification
1st Stage 5a Tirreno–Adriatico
3rd GP van Malderen
8th Paris–Tours
9th Amstel Gold Race
10th Brussel-Ingooigem
1973
1st Paris–Tours
Giro d'Italia
1st Stages 7 & 17
Paris–Nice
1st Stages 2, 3b (TTT), 5 & 5a
Tour of Belgium
1st Prologue (TTT)
Giro di Sardegna
1st Stages 1, 2 & 4b
1st Puivelde Koerse
2nd Grand Prix Pino Cerami
3rd Overall Vuelta a Andalucía
1st Prologue & Stages 1, 4 & 6
3rd Paris–Brussels
4th Milan–San Remo
10th E3 Harelbeke
1974
1st Overall Giro di Sardegna
Vuelta a España
1st Stages 3 & 4
10th Overall Paris–Nice
1st Points Classification
1st Stage 7a
1st Omloop der Zuid-West-Vlaamse Bergen
2nd Grote Prijs Jef Scherens
2nd Omloop Schelde-Durme
3rd Omloop Het Vol |
https://en.wikipedia.org/wiki/Raymond%20Martin%20%28cyclist%29 | Raymond Martin (born 22 May 1949) is a former French road bicycle racer. In the 1980 Tour de France he finished third overall and won the mountains classification. He also competed in the individual road race at the 1972 Summer Olympics.
Major results
1972
National Amateur Road Race Championship
1974
GP Ouest-France
Lescouet-Jugon
Route Niveroise
1975
Paris–Camembert
1978
Grand Prix de Plumelec-Morbihan
Josselin
1979
Paris–Camembert
1980
Agon-Coutainville
Lescouet-Jugon
Trophée des Grimpeurs
Tour de France:
Winner stage 13
Winner mountains classification
3rd place overall classification
1982
Tour de France:
8th place overall classification
References
External links
Official Tour de France results for Raymond Martin (cyclist)
1949 births
Living people
French male cyclists
French Tour de France stage winners
Olympic cyclists for France
Cyclists at the 1972 Summer Olympics
Sportspeople from Orne
Cyclists from Normandy |
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