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https://en.wikipedia.org/wiki/Bernard%20Vallet | Bernard Vallet (born January 18, 1954 in Vienne, Isère) is a French former road bicycle racer who won the mountains classification in the 1982 Tour de France.
From 2003 to 2011, Bernard Vallet was the analyst of the Tour de France on Canal Evasion with the two sports commentator Richard Garneau and Louis Bertrand. Moreover, he is the analyst for the Quebec broadcasting of Grand Prix Cycliste de Montréal et Grand Prix Cycliste de Québec since the first edition.
Major results
1968
National Amateur Road Race Championship
1977
Mende
1979
Tour du Limousin
1980
GP de la Ville de Rennes
Mende
Niort
Six Days of Nouméa (with Maurizio Bidinost)
Tour de France:
Winner stage 15
1981
Arras
Circuit des genêts verts
Maël-Pestivien
Tour d'Armorique
1982
Bain-de-Bretagne
Chamalières
Six-Days of Grenoble (with Gert Frank)
Lescouet-Jugon
Ronde Aude
Tour de France:
Winner mountains classification
1984
Camors
Six-Days of Grenoble (with Gert Frank)
National Track Points Race Championship
Six Days of Paris (with Gert Frank)
1985
Clermont-Ferrand
Marthon
1986
Bussières
Six Days of Paris (with Danny Clark)
Poitiers
1987
Joué-les-Tours
Bordeaux–Paris
Les Ormes
Castillon-la-Bataille
Six-Days of Grenoble (with Charly Mottet)
External links
Official Tour de France results for Bernard Vallet
1954 births
Living people
Sportspeople from Vienne, Isère
Cyclists from Isère
French male cyclists
French Tour de France stage winners |
https://en.wikipedia.org/wiki/Superstatistics | Superstatistics is a branch of statistical mechanics or statistical physics devoted to the study of non-linear and non-equilibrium systems. It is characterized by using the superposition of multiple differing statistical models to achieve the desired non-linearity. In terms of ordinary statistical ideas, this is equivalent to compounding the distributions of random variables and it may be considered a simple case of a doubly stochastic model.
Consider an extended thermodynamical system which is locally in equilibrium and has a Boltzmann distribution, that is the probability of finding the system in a state with energy is proportional to . Here is the local inverse temperature. A non-equilibrium thermodynamical system is modeled by considering macroscopic fluctuations of the local inverse temperature. These fluctuations happen on time scales which are much larger than the microscopic relaxation times to the Boltzmann distribution. If the fluctuations of are characterized by a distribution , the superstatistical Boltzmann factor of the system is given by
This defines the superstatistical partition function
for system that can assume discrete energy states . The probability of finding the system in state is then given by
Modeling the fluctuations of leads to a description in terms of statistics of Boltzmann statistics, or "superstatistics". For example, if follows a Gamma distribution, the resulting superstatistics corresponds to Tsallis statistics. Superstatistics can |
https://en.wikipedia.org/wiki/AP1S1 | AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the AP1S1 gene.
Function
The protein encoded by this gene is part of the clathrin coat assembly complex which links clathrin to receptors in coated vesicles. These vesicles are involved in endocytosis and Golgi processing. This protein, as well as beta-prime-adaptin, gamma-adaptin, and the medium (mu) chain AP47, form the AP-1 assembly protein complex located at the Golgi vesicle. Two alternatively spliced transcript variants of this gene, which encode distinct isoforms, have been reported.
A mutation in the AP1S1 causes the rare familial MEDNIK syndrome described in 2008.
Interactions
AP1S1 has been shown to interact with AP1G1 and RAB10.
References
Further reading
External links |
https://en.wikipedia.org/wiki/CLNS1A | Methylosome subunit pICln is a protein that in humans is encoded by the CLNS1A gene.
Interactions
CLNS1A has been shown to interact with:
ITGA2B,
PRMT5,
SNRPD1, and
SNRPD3.
See also
Chloride channel
References
Further reading
External links
Ion channels |
https://en.wikipedia.org/wiki/Cyclic%20nucleotide-gated%20channel%20alpha%203 | Cyclic nucleotide-gated cation channel alpha-3 is a protein that in humans is encoded by the CNGA3 gene.
Function
This gene encodes a member of the cyclic nucleotide-gated cation channel protein family, which is required for normal vision and olfactory signal transduction. CNGA3 is expressed in cone photoreceptors and is necessary for color vision. Missense mutations in this gene are associated with rod monochromacy and segregate in an autosomal recessive pattern. Two alternatively-spliced transcripts encoding different isoforms have been described.
Clinical relevance
Variants in this gene have been shown to cause achromatopsia and colour blindness.
See also
Cyclic nucleotide-gated ion channel
References
Further reading
External links
GeneReviews/NIH/NCBI/UW entry on Achromatopsia
OMIM entries on Achromatopsia
Ion channels |
https://en.wikipedia.org/wiki/Collagen%2C%20type%20XI%2C%20alpha%201 | Collagen alpha-1(XI) chain is a protein that in humans is encoded by the COL11A1 gene.
Function
The COL11A1 gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. Type XI collagen is a heterotrimer but the third alpha chain is a post-translationally modified alpha 1 type II chain. Three transcript variants encoding different isoforms have been identified for this gene.
Clinical significance
Mutations in this gene are associated with type II Stickler syndrome and with Marshall syndrome.
Stickler syndrome, type II is an autosomal dominant condition caused by a mutation in the COL11A1 gene. Features of Stickler syndrome type II include: sensorineural hearing loss, facial features (flat facial profile, anteverted nares, micrognathia), cleft palate, visual disturbances (type 2 vitreous anomaly, childhood-onset myopia, glaucoma, cataracts and retinal detachment), spondyloepiphyseal dysplasia, and arthropathy.
References
External links
GeneReviews/NCBI/NIH/UW entry on Stickler Syndrome
Further reading |
https://en.wikipedia.org/wiki/High%20affinity%20copper%20uptake%20protein%201 | High affinity copper uptake protein 1 (CTR1) is a protein that in humans is encoded by the SLC31A1 gene.
Copper is an element essential for life, but excessive copper can be toxic or even lethal to the cell. Therefore, cells have developed sophisticated ways to maintain a critical copper balance, with the intake, export, and intracellular compartmentalization or buffering of copper strictly regulated. The 2 related genes ATP7A and ATP7B, responsible for the human diseases Menkes syndrome and Wilson disease, respectively, are involved in copper export. In S. cerevisiae, the copper uptake genes CTR1, CTR2, and CTR3 have been identified, and in human the CTR1 and CTR2 (MIM 603088) genes have been identified.
Clinical significance
In 2022, a new autosomal-recessive disease was discovered that is caused by mutations of the CTR1 gene. The disease is characterized by profound deficiency of copper in the central nervous system and presents with infantile seizures and neurodegeneration.
See also
Solute carrier family
References
Further reading
Solute carrier family |
https://en.wikipedia.org/wiki/CRYBB1 | Beta-crystallin B1 is a protein that in humans is encoded by the CRYBB1 gene. Variants in CRYBB1 are associated with autosomal dominant congenital cataract.
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins.
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions.
Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta basic group member, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3.
References
External links
Further reading |
https://en.wikipedia.org/wiki/CRYGB | Gamma-crystallin B is a protein that in humans is encoded by the CRYGB gene.
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins.
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions.
Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
References
External links
Further reading |
https://en.wikipedia.org/wiki/DGUOK | Deoxyguanosine kinase, mitochondrial is an enzyme that in humans is encoded by the DGUOK gene.
Function
In mammalian cells, the phosphorylation of purine deoxyribonucleosides is mediated predominantly by two deoxyribonucleoside kinases, cytosolic deoxycytidine kinase and mitochondrial deoxyguanosine kinase. The protein encoded by this gene is responsible for phosphorylation of purine deoxyribonucleosides in the mitochondrial matrix. In addition, this protein phosphorylates several purine deoxyribonucleoside analogs used in the treatment of lymphoproliferative disorders, and this phosphorylation is critical for the effectiveness of the analogs. Alternative splice variants encoding different protein isoforms have been described for this gene.
Clinical
Mutations in this gene have been linked to inherited mitochondrial DNA depletion syndromes, neonatal liver failure, nystagmus and hypotonia.
References
Further reading
External links
GeneReview/NIH/UW entry on DGUOK-Related Mitochondrial DNA Depletion Syndrome, Hepatocerebral Form |
https://en.wikipedia.org/wiki/DLX3 | Homeobox protein DLX-3 is a protein that in humans is encoded by the DLX3 gene.
Function
Dlx3 is a crucial regulator of hair follicle differentiation and cycling. Dlx3 transcription is mediated through Wnt, and colocalization of Dlx3 with phospho-SMAD1/5/8 is involved in the regulation of transcription by BMP signaling. Dlx3 transcription is also induced by BMP-2 through transactivation with SMAD1 and SMAD4.
Many vertebrate homeo box-containing genes have been identified on the basis of their sequence similarity with Drosophila developmental genes. Members of the Dlx gene family contain a homeobox that is related to that of Distal-less (Dll), a gene expressed in the head and limbs of the developing fruit fly. The Distal-less (Dlx) family of genes comprises at least 6 different members, DLX1-DLX6. This gene is located in a tail-to-tail configuration with another member of the gene family on the long arm of chromosome 17.
Clinical significance
Mutations in this gene have been associated with the autosomal dominant conditions trichodentoosseous syndrome (TDO) and amelogenesis imperfecta with taurodontism.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/DSC3 | Desmocollin-3 is a protein that in humans is encoded by the DSC3 gene.
Gene
The desmosomal family members are arranged in two clusters on chromosome 18, occupying less than 650 kb combined. Alternative splicing results in two transcript variants encoding distinct isoforms.
Function
Desmocollin-3 is a calcium-dependent glycoprotein that is a member of the desmocollin subfamily of the cadherin superfamily. These desmosomal family members, along with the desmogleins, are found primarily in epithelial cells where they constitute the adhesive proteins of the desmosome cell-cell junction and are required for cell adhesion and desmosome formation. The loss of these components leads to a lack of adhesion and a gain of cellular mobility.
Clinical significance
Breast cancer
Through the process of epigenetic silencing, the expression of the desmocollin-3 protein is down regulated in many breast cancers.
Hereditary hypotrichosis
A consanguineous Afghan family in which 3 sisters, 12 to 18 years of age, and their 5-year-old brother displayed features of hereditary hypotrichosis, associated with vesicles on the scalp and skin. At birth, scalp hair was present, and after ritual shaving at 1 week of age, scalp hair grew back; however, the hair was fragile and began falling out at 2 to 3 months of age, eventually leaving only sparse hair on the scalp. Vesicles that were less than 1 cm in diameter were observed on the scalp and skin of most of the body, occasionally disappearing bu |
https://en.wikipedia.org/wiki/E2F5 | Transcription factor E2F5 is a protein that in humans is encoded by the E2F5 gene.
Function
The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionarily conserved domains that are present in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein is differentially phosphorylated and is expressed in a wide variety of human tissues. It has higher identity to E2F4 than to other family members. Both this protein and E2F4 interact with tumor suppressor proteins p130 and p107, but not with pRB. Alternative splicing results in multiple variants encoding different isoforms.
Interactions
E2F5 has been shown to interact with TFDP1.
See also
E2F
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/IL18BP | Interleukin-18-binding protein is a protein that in humans is encoded by the IL18BP gene.
The protein encoded by this gene is an inhibitor of the proinflammatory cytokine IL18. This protein binds to IL18, prevents the binding of IL18 to its receptor, and thus inhibits IL18-induced IFN-gamma production. This protein is constitutively expressed and secreted in mononuclear cells. The expression of this protein can be enhanced by IFN-gamma. An elevated level of this protein is detected in the intestinal tissues of patients with Crohn's disease. Three transcript variants encoding the same protein have been found for this gene.
References
Further reading
External links |
https://en.wikipedia.org/wiki/ALYREF | Aly/REF export factor, also known as THO complex subunit 4 is a protein that in humans is encoded by the ALYREF gene.
The ALYREF gene encodes Aly/REF export factor (ALY; THO complex subunit 4, Tho4; RNA and export factor binding protein 1, Refbp1), a ubiquitously expressed nuclear protein that functions as a molecular chaperone and export adapter involved in nuclear export of spliced and unspliced mRNA. The TRanscription-EXport (TREX) complex, a key player in mRNA export, includes the THO subcomplex, the RNA helicase UAP56, and the RNA-binding protein ALY. In yeast, TREX is recruited co-transcriptionally; in human cells it is recruited during a late step of splicing. The human TREX complex is recruited to a region near the 5' end of mRNA by interaction of ALY and THO with the nuclear cap-binding complex. As a chaperone, ALY promotes dimerization of transcription factors containing basic leucine zipper (bZIP) domains., thereby promoting transcriptional activation. ALY has key roles in 3'-end processing of polyadenylated mRNAs and in nuclear export of both polyadenylated and non-polyadenylated mRNAs. After mRNA binds to ALY, it is apparently transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). The full-length ALY protein (Refbp1-I, 255 amino acids encoded by six exons) has a conserved RNA recognition motif (RRM; amino acids 105-182) flanked by alanine/arginine/glycine-rich sequences; an N-terminal region (amino acids 16-37) is sufficient for RNA binding and |
https://en.wikipedia.org/wiki/Tubulin%20beta-4A%20chain | Tubulin beta-4A chain is a protein that in humans is encoded by the TUBB4A gene. Two tubulin beta-4 chain proteins are encoded in the human genome by the genes TUBB4A (this entry) and TUBB4B. Tubulin is the major constituent of microtubules, a key components of the cytoskeleton. It binds two molecules of GTP, one at an exchangeable site on the beta-chain and one at a non-exchangeable site on the alpha-chain. TUBB4A is preferentially and highly expressed in the central nervous system.
Clinical significance
Mutations in TUBB4A have been associated with two neurological disorders.
An R2G substitution in the autoregulatory MREI domain of TUBB4A has been identified as the cause of 'hereditary whispering dysphonia' or DYT4.
A de novo D249N mutation has been identified as the cause of a rare leukoencephalopathy, hypomyelination with atrophy of basal ganglia and cerebellum (H-ABC).
Mutations in TUBB4A are associated with Pelizaeus–Merzbacher disease.
References
Further reading
External links |
https://en.wikipedia.org/wiki/GPNMB | Transmembrane glycoprotein NMB is a protein that in humans is encoded by the GPNMB gene. Two transcript variants encoding 560 and 572 amino acid isoforms have been characterized for this gene in humans. The mouse and rat orthologues of GPNMB are known as DC-HIL and Osteoactivin (OA), respectively.
GPNMB is a type I transmembrane glycoprotein which shows homology to the pmel17 precursor, a melanocyte-specific protein.
GPNMB has been reported to be expressed in various cell types, including: melanocytes, osteoclasts, osteoblasts, dendritic cells, and it is overexpressed in various cancer types. In melanocytic cells and osteoclasts the GPNMB gene is transcriptionally regulated by Microphthalmia-associated transcription factor.
Function
In osteoblast progenitor cells, Osteoactivin works as a positive regulator of osteoblast differentiation during later stages of matrix maturation and mineralization that is mediated at least in part by Bone_morphogenetic_protein_2 in a SMAD1 dependent manner to promote osteoblast differentiation. In addition, using a rat fracture model, Osteoactivin (OA) enhances the repairing process in bone fracture, demonstrated by its high expression during chondrogenesis (soft callus) and osteogenesis (hard callus) compared to the intact femurs that is why Osteoactivin (OA) could be a novel therapeutic agent used to treat generalized osteoporosis or localized osteopenia during fracture repair by stimulating bone growth and regeneration. Similarly, Osteoac |
https://en.wikipedia.org/wiki/HYOU1 | Hypoxia up-regulated protein 1 is a protein that in humans is encoded by the HYOU1 gene.
The protein encoded by this gene belongs to the heat shock protein 70 family. This gene has three mRNAs from the use of alternative transcription sites. A cis-acting segment is found at the 5' end of exon 1A which is involved in the stress-dependent induction. The transcript that begins with exon 1B is preferentially induced by hypoxia, resulting in the accumulation of this protein in the endoplasmic reticulum (ER).
The protein encoded by this gene is thought to play an important role in protein folding and secretion in the ER. Since suppression of the protein is associated with accelerated apoptosis, it is also suggested to have an important cytoprotective role in hypoxia-induced cellular perturbation. This protein has been shown to be up-regulated in tumors, especially in breast tumors, and thus it is associated with tumor invasiveness.
There is also an alternative translation site of this gene which lacks the signal peptide. This signal peptide-lacking protein, is only 3 amino acids shorter than the mature protein in the ER, and it is thought to have a housekeeping function in the cytosol.
References
Further reading |
https://en.wikipedia.org/wiki/IGF2BP3 | Insulin-like growth factor 2 mRNA-binding protein 3 is a protein that in humans is encoded by the IGF2BP3 gene.
The protein encoded by this gene is primarily found in the nucleolus, where it can bind to the 5' UTR of the insulin-like growth factor II leader 3 mRNA and may repress translation of insulin-like growth factor II during late development.
The encoded protein contains several KH domains, which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. A pseudogene exists on chromosome 7, and there are putative pseudogenes on other chromosomes.
See also
IGF2BP1
IGF2BP2
References
Further reading |
https://en.wikipedia.org/wiki/FUSIP1 | FUS-interacting serine-arginine-rich protein 1 is a protein that in humans is encoded by the SFRS13A gene.
Function
This gene product is a member of the serine-arginine (SR) family of proteins, which is involved in constitutive and regulated RNA splicing. Members of this family are characterized by N-terminal RNP1 and RNP2 motifs, which are required for binding to RNA, and multiple C-terminal SR/RS repeats, which are important in mediating association with other cellular proteins. This protein can influence splice site selection of adenovirus E1A pre-mRNA. It interacts with the oncoprotein TLS and abrogates the influence of TLS on E1A pre-mRNA splicing. Alternative splicing of this gene results in at least two transcript variants encoding different isoforms. In addition, transcript variants utilizing alternative polyA sites exist.
Interactions
FUSIP1 has been shown to interact with FUS.
References
Further reading |
https://en.wikipedia.org/wiki/CPLX2 | Complexin-2 is a protein that in humans is encoded by the CPLX2 gene.
Proteins encoded by the complexin/synaphin gene family are cytosolic proteins that function in synaptic vesicle exocytosis. These proteins bind syntaxin, part of the SNAP receptor. The protein product of this gene binds to the SNAP receptor complex and disrupts it, allowing transmitter release. Two transcript variants encoding the same protein have been found for this gene.
References
External links
Further reading |
https://en.wikipedia.org/wiki/EHD1 | EH domain-containing protein 1, also known as testilin or PAST homolog 1 (PAST1), is a protein that in humans is encoded by the EHD1 gene belonging to the EHD protein family.
Function
This gene belongs to a highly conserved gene family encoding EPS15 homology (EH) domain-containing proteins. The protein-binding EH domain was first noted in EPS15, a substrate for the epidermal growth factor receptor. The EH domain has been shown to be an important motif in proteins involved in protein-protein interactions and in intracellular sorting. The protein encoded by this gene is thought to play a role in the endocytosis of IGF1 receptors.
Interactions
EHD1 has been shown to interact with Insulin-like growth factor 1 receptor and SNAP29.
References
Further reading
EH-domain-containing proteins |
https://en.wikipedia.org/wiki/LILRB4 | Leukocyte immunoglobulin-like receptor subfamily B member 4 is a protein that in humans is encoded by the LILRB4 gene.
This gene is a member of the leukocyte immunoglobulin-like receptor (LIR) family, which is found in a gene cluster at chromosomal region 19q13.4. The encoded protein belongs to the subfamily B class of LIR receptors which contain two or four extracellular immunoglobulin domains, a transmembrane domain, and two to four cytoplasmic immunoreceptor tyrosine-based inhibitory motifs (ITIMs). The receptor is expressed on monocytic cells and transduces a negative signal that inhibits stimulation of an immune response. The receptor can also function in antigen capture and presentation. It is thought to control inflammatory responses and cytotoxicity to help focus the immune response and limit autoreactivity. LILRB4 has also been proposed to be a potential target for tumor immunotherapy. It has been shown to express on tumor-associated macrophages and negatively regulate immune response in tumor. The expression of LILRB4 on monocytic myeloid leukemia cells supports infiltration and inhibits T cell proliferation. Multiple transcript variants encoding different isoforms have been found for this gene.
Interactions
LILRB4 has been shown to interact with PTPN6 and INPP5D (SHIP-1).
See also
Cluster of differentiation
Immunoglobulin superfamily
References
Further reading
External links
Clusters of differentiation
Immunoglobulin superfamily |
https://en.wikipedia.org/wiki/KLK11 | Kallikrein-11 is a protein that in humans is encoded by the KLK11 gene.
Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. Alternate splicing of this gene results in two transcript variants encoding two different isoforms which are differentially expressed.
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: S01.257 |
https://en.wikipedia.org/wiki/EGLN3 | Egl nine homolog 3 is a protein that in humans is encoded by the EGLN3 gene. ELGN3 is a member of the superfamily of alpha-ketoglutarate-dependent hydroxylases, which are non-haem iron-containing proteins.
References
Further reading
Human 2OG oxygenases
EC 1.14.11 |
https://en.wikipedia.org/wiki/CENTG1 | Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2 is a protein that in humans is encoded by the AGAP2 gene.
Interactions
CENTG1 has been shown to interact with:
EPB41L1,
HOMER1 and
PIK3R1.
References
External links
Further reading |
https://en.wikipedia.org/wiki/EPB41L1 | Band 4.1-like protein 1 is a protein that in humans is encoded by the EPB41L1 gene.
Function
Erythrocyte membrane protein band 4.1 (EPB41) is a multifunctional protein that mediates interactions between the erythrocyte cytoskeleton and the overlying plasma membrane. The protein encoded by this gene is a neuronally-enriched protein that is structurally similar to EPB41. The encoded protein binds and stabilizes D2 and D3 dopamine receptors at the neuronal plasma membrane. Multiple transcript variants encoding different isoforms have been found for this gene, but the full-length nature of only two of them has been determined.
Interactions
EPB41L1 has been shown to interact with:
CENTG1,
Dopamine receptor D2,
Dopamine receptor D3,
ITPR1, and
Nuclear mitotic apparatus protein 1.
References
Further reading |
https://en.wikipedia.org/wiki/EPRS | Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS gene.
Gene
Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined.
Function
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species.
Phosphorylation of EPRS is reported to be essential for the formation of GAIT (Gamma-interferon Activated Inhibitor of Translation) complex that regulates the translation of multiple genes in monocytes and macrophages.
Interactions
EPRS has been shown to interact with POU2F1, Heat shock protein 90kDa alpha (cytosolic), member A1 and IARS.
References
Further reading |
https://en.wikipedia.org/wiki/FANCF | Fanconi anemia group F protein is a protein that in humans is encoded by the FANCF gene.
Interactions
FANCF has been shown to interact with Fanconi anemia, complementation group C, FANCG, FANCA and FANCE.
Function
FANCF is an adaptor protein that plays a key role in the proper assembly of the FA core complex. The FA core complex is composed of eight proteins (FANCA, -B, -C, -E, -F, -G, -L and -M). FANCF stabilizes the interaction between the FANCC/FANCE subcomplex and the FANCA/FANCG subcomplex and locks the whole FA core complex in a conformation that is essential to perform its function in DNA repair.
The FA core complex is a nuclear core complex that is essential for the monoubiquitination of FANCD2 and this modified form of FANCD2 colocalizes with BRCA1, RAD51 and PCNA in foci that also contain other DNA repair proteins. All these proteins function together to facilitate DNA interstrand cross-link repair. They also function in other DNA damage response repair processes including recovering and stabilizing stalled replication forks. FoxF1 protein also interacts with the FA protein core and induces its binding to chromatin to promote DNA repair.
Cancer
DNA damage appears to be the primary underlying cause of cancer, and deficiencies in expression of DNA repair genes appear to underlie many forms of cancer. If DNA repair is deficient, DNA damage tends to accumulate. Such excess DNA damage may increase mutations due to error-prone translesion synthesis. Excess DN |
https://en.wikipedia.org/wiki/Adrenal%20ferredoxin | Adrenal ferredoxin (also adrenodoxin (ADX), adrenodoxin, mitochondrial, hepatoredoxin, ferredoxin-1 (FDX1)) is a protein that in humans is encoded by the FDX1 gene. In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21.
Function
Adrenodoxin is a small iron-sulfur protein that can accept and carry a single electron. Adrenodoxin functions as an electron transfer protein in the mitochondrial cytochrome P450 systems. The first enzyme in this system is adrenodoxin reductase that carries an FAD. FAD can be reduced by two electrons donated from coenzyme NADPH. These two electrons are transferred one a time to adrenodoxin. Adrenodoxin in return reduces mitochondrial cytochrome P450. This particular oxidation/reduction system is involved in the synthesis of steroid hormones in steroidogenic tissues. In addition, similar systems also function in vitamin D and bile acid synthesis in the kidney and liver respectively. Adrenodoxin has been identified in a number of different tissues but all forms have been shown to be identical and are not tissue specific.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Adrenodoxin%20reductase | Adrenodoxin reductase (Enzyme Nomenclature name: adrenodoxin-NADP+ reductase, EC 1.18.1.6), was first isolated from bovine adrenal cortex where it functions as the first enzyme in the mitochondrial P450 systems that catalyze essential steps in steroid hormone biosynthesis.
Examination of complete genome sequences revealed that adrenodoxin reductase gene is present in most metazoans and prokaryotes.
Nomenclature
The name of the enzyme was coined based on its function to reduce a [2Fe-2S] (2 iron, 2 sulfur) electron-transfer protein that was named adrenodoxin. Later, in some studies, the enzyme was also referred to as a "ferredoxin reductase", as adrenodoxin is a ferredoxin. In the human gene nomenclature, the standard name is ferredoxin reductase and the symbol is FDXR, with ADXR specified as a synonym.
The assignment of the name "ferredoxin reductase" has been criticized as a misnomer because determination of the structure of adrenodoxin reductase revealed that it is completely different from that of plant ferredoxin reductase and there is no homology between these two enzymes. With more proteins with a ferroxodin-reducing activity discovered in both families as well as novel families, this enzyme activity is now seen as an example of convergent evolution.
Function
Adrenodoxin reductase is a flavoprotein as it carries a FAD type coenzyme. The enzyme functions as the first electron transfer protein of mitochondrial P450 systems such as P450scc. The FAD coenzyme receives |
https://en.wikipedia.org/wiki/Flavin%20containing%20monooxygenase%201 | Dimethylaniline monooxygenase [N-oxide-forming] 1 is an enzyme that in humans is encoded by the FMO1 gene.
Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in humans resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome Trimethylaminuria. Three forms of the enzyme, FMO1 found in fetal liver, FMO2 found in adult liver, and FMO3 are encoded by genes clustered in the 1q23-q25 region. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in xenobiotics such as pesticides and drugs.
References
Further reading |
https://en.wikipedia.org/wiki/FUT7 | Alpha-(1,3)-fucosyltransferase is an enzyme that in humans is encoded by the FUT7 gene.
Function
The sialyl Lewis x oligosaccharide determinant is an essential component of leukocyte counterreceptors for E-selectin- (MIM 131210) and P-selectin- (MIM 173610) mediated adhesions of leukocytes. This oligosaccharide molecule is displayed on the surfaces of granulocytes, monocytes, and natural killer cells. Formation of leukocyte adhesions to these selectins is an early and important step in the process that ultimately allows leukocytes to leave the vascular tree and become recruited into lymphoid tissues and sites of inflammation.[supplied by OMIM]
References
Further reading |
https://en.wikipedia.org/wiki/GALNT3 | Polypeptide N-acetylgalactosaminyltransferase 3 is an enzyme that in humans is encoded by the GALNT3 gene.
This gene encodes UDP-GalNAc transferase 3, a member of the polypeptide GalNAc transferase (GalNAc-T) family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. Individual GalNAc-transferases have distinct activities and initiation of O-glycosylation is regulated by a repertoire of GalNAc-transferases. The protein encoded by this gene is highly homologous to other family members; however, the enzymes have different substrate specificities.
References
Further reading |
https://en.wikipedia.org/wiki/GNRH2 | Progonadoliberin-2 is a protein that in humans is encoded by the GNRH2 gene.
The protein encoded by this gene is a preproprotein that is cleaved to form a secreted 10 aa peptide hormone, QHWSHGWYPG. The secreted decapeptide regulates reproduction in females by stimulating the secretion of both luteinizing- and follicle-stimulating hormones. Three transcript variants that encode unique proproteins but the same peptide hormone have been found for this gene. The peptide belongs to gonadotropin-releasing hormone family.
References
Further reading
Precursor proteins
Decapeptides |
https://en.wikipedia.org/wiki/GOT2 | Aspartate aminotransferase, mitochondrial is an enzyme that in humans is encoded by the GOT2 gene. Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2, respectively. GOT plays a role in amino acid metabolism and the urea and Kreb's cycle. Also, GOT2 is a major participant in the malate-aspartate shuttle, which is a passage from the cytosol to the mitochondria. The two enzymes are homodimeric and show close homology. GOT2 has been seen to have a role in cell proliferation, especially in terms of tumor growth.
Structure
GOT2 is a dimer containing two identical subunits that hold overlapping subunit regions. The top and sides of the enzyme are made up of helices, while the bottom is formed by strands of beta sheets and extended hairpin loops. The subunit itself can be categorized into four different parts: a large domain, which binds pyridoxal-P, a small domain, an NH2-terminal arm, and a bridge across two domains, which is formed by residues 48-75 and 301-358. Virtually ubiquitous in eukaryotic cells, GOT2 nucleic acid and protein sequences are highly conserved, and its 5’regulatory regions in genomic DNA resemble those of typical house-keeping genes in that, e.g., they lack a TATA box. The GOT2 gene is also located on 16q21 and has an exon count of 10.
Function
In order to produce the energy needed for everyday activities, our body needs to go through the process of |
https://en.wikipedia.org/wiki/GRK4 | G protein-coupled receptor kinase 4 (GRK4) is an enzyme that is encoded by the GRK4 gene in humans.
This gene encodes a member of the G protein-coupled receptor kinase subfamily of the Ser/Thr protein kinase family, and is most similar to GRK5 and GRK6.
G protein-coupled receptor kinases phosphorylate activated G protein-coupled receptors, which promotes the binding of an arrestin protein to the receptor. Arrestin binding to a phosphorylated, active receptor prevents receptor stimulation of heterotrimeric G protein transducer proteins, blocking their cellular signaling and resulting in receptor desensitization. Moreover Arrestin binding to a phosphorylated, active receptor also enables receptor signaling through arrestin partner proteins. Consequently the GRK/arrestin system serves as a signaling switch for G protein-coupled receptors.
GRK4 is most highly expressed in the testes, with lower amounts found in the brain, kidney and other tissues. It exists in four alternatively-spliced variants.
Polymorphisms in the GRK4 gene have been linked to both genetic and acquired hypertension, partly acting through kidney dopamine receptors.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/RAB18 | Ras-related protein Rab-18 is a protein that in humans is encoded by the RAB18 gene. It is a member of the Rab family of Ras-related small GTPases.
Rab18 is a ubiquitously expressed protein with particularly high expression in the brain. Rab18 was first characterised as an endosomal protein in epithelial cells of mouse kidney and intestines. Subsequent studies revealed that Rab18 has a wide intracellular distribution; localising to the Golgi complex, endoplasmic reticulum, lipid droplets, and cytosol of various cell types. In the brain, Rab18 has been isolated in association with synaptic vesicles and has been observed to localise to secretory granules in neuroendocrine cells.
Mutations in RAB18, RAB3GAP1, RAB3GAP2, or TBC1D20 are thought to cause Warburg Micro syndrome by disrupting RAB18 function. RAB3GAP1, RAB3GAP2, and TBC1D20 genes offer instructions for creating proteins that regulate RAB18. The RAB3GAP1 and RAB3GAP2 proteins interact and create a guanine–nucleotide exchange factor complex that activates RAB18. The TBC1D20 protein may inactivate RAB18 by acting as a GTPase-activating protein for it.
References
Further reading |
https://en.wikipedia.org/wiki/SHANK2 | SH3 and multiple ankyrin repeat domains protein 2 is a protein that in humans is encoded by the SHANK2 gene. Two alternative splice variants, encoding distinct isoforms, are reported. Additional splice variants exist but their full-length nature has not been determined.
Function
This gene encodes a protein that is a member of the Shank family of synaptic proteins that may function as molecular scaffolds in the postsynaptic density (PSD). Shank proteins contain multiple domains for protein-protein interaction, including ankyrin repeats, an SH3 domain, a PSD-95/Dlg/ZO-1 domain, a sterile alpha motif domain, and a proline-rich region. This particular family member contains a PDZ domain, a consensus sequence for cortactin SH3 domain-binding peptides and a sterile alpha motif. The alternative splicing demonstrated in Shank genes has been suggested as a mechanism for regulating the molecular structure of Shank and the spectrum of Shank-interacting proteins in the PSDs of adult and developing brain.
It is thought that SHANK2 might play a role in synaptogenesis by attaching metabotropic glutamate receptors (mGluRs) to an existing pool of NMDA receptors (NMDA-R), bylinking to the NMDA-R through PSD-95, and the mGluRs through HOMER1. An alternative hypothesis is that the Homer/Shank/GKAP/PSD-95 assembly mediates physical association of the NMDAR with IP3R/RYR and intracellular Ca2+ stores.
Interactions
SHANK2 has been shown to interact with:
ARHGEF7,
Cortactin,
DLG4,
DLGAP1, |
https://en.wikipedia.org/wiki/PEG10 | Retrotransposon-derived protein PEG10 is a protein that in humans is encoded by the PEG10 gene.
Function
This gene includes two overlapping reading frames of the same transcript encoding distinct isoforms. The shorter isoform has a CCHC-type zinc finger motif containing a sequence characteristic of gag proteins of most retroviruses and some retrotransposons, and it functions in part by interacting with members of the TGF-beta receptor family. The longer isoform has the active-site DSG consensus sequence of the protease domain of pol proteins. The longer isoform is the result of -1 translational frameshifting that is also seen in some retroviruses. Expression of these two isoforms only comes from the paternal allele due to imprinting. Increased gene expression (as observed by an increase in mRNA levels) is associated with hepatocellular carcinomas.
PEG10 is a paternally expressed imprinted gene that is expressed in adult and embryonic tissues. Most notable expression occurs in the placenta. This gene is highly conserved across mammalian species and retains the heptanucleotide (GGGAAAC). This gene has been reported to play a role in cell proliferation, differentiation and apoptosis. Overexpression of this gene has been associated with several malignancies, such as hepatocellular carcinoma and B-cell lymphocytic leukemia. Knockout mice lacking this gene showed early embryonic lethality with placental defects, indicating the importance of this gene in embryonic development. I |
https://en.wikipedia.org/wiki/ARHGEF12 | Rho guanine nucleotide exchange factor 12 is a protein that in humans is encoded by the ARHGEF12 gene. This protein is also called RhoGEF12 or Leukemia-associated Rho guanine nucleotide exchange factor (LARG).
Function
Rho guanine nucleotide exchange factor 12 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.
RhoGEF12 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), ARHGEF11 (also known as PDZ-RhoGEF) and AKAP13 (also known as ARHGEF13 and Lbc). GPCR-regulated RhoGEF12 (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 |
https://en.wikipedia.org/wiki/HEY2 | Hairy/enhancer-of-split related with YRPW motif protein 2 (HEY2) also known as cardiovascular helix-loop-helix factor 1 (CHF1) is a protein that in humans is encoded by the HEY2 gene.
This protein is a type of transcription factor that belongs to the hairy and enhancer of split-related (HESR) family of basic helix-loop-helix (bHLH)-type transcription factors. It forms homo- or hetero-dimers that localize to the nucleus and interact with a histone deacetylase complex to repress transcription. During embryonic development, this mechanism is used to control the number of cells that develop into cardiac progenitor cells and myocardial cells. The relationship is inversely related, so as the number of cells that express the Hey2 gene increases, the more CHF1 is present to repress transcription and the number of cells that take on a myocardial fate decreases.
Expression
The expression of the Hey2 gene is induced by the Notch signaling pathway. In this mechanism, adjacent cells bind via transmembrane notch receptors. Two similar and redundant genes in mouse are required for embryonic cardiovascular development, and are also implicated in neurogenesis and somitogenesis. Alternatively spliced transcript variants have been found, but their biological validity has not been determined.
Knockout studies
The Hey2 gene is involved with the formation of the cardiovascular system and especially the heart itself. Although studies have not been conducted about the effects of a malfunc |
https://en.wikipedia.org/wiki/Caspase%2014 | Caspase 14 is an enzyme that in humans is encoded by the CASP14 gene.
The CASP14 gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This caspase has been shown to be processed and activated by caspase 8 and caspase 10 in vitro, and by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this caspase may be involved in keratinocyte terminal differentiation, which is important for the formation of the skin barrier.
According to the Human Protein Atlas, the CASP14 protein is enriched human skin and mainly expressed in the upper layers of the epidermis. The protein is mainly localised to the cytosol according to the Cell Atlas.
See also
The Proteolysis Map
Caspase
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: C14.018
Caspases |
https://en.wikipedia.org/wiki/PRND | Prion protein 2 (dublet), also known as PRND, or Doppel protein, is a protein which in humans is encoded by the PRND gene.
Function
This gene is found on chromosome 20, approximately 20 kbp downstream of the gene encoding cellular prion protein, to which it is biochemically and structurally similar. The protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that is found predominantly in testis. Mutations in this gene may lead to neurological disorders.
References
Further reading |
https://en.wikipedia.org/wiki/NOC2L | Nucleolar complex protein 2 homolog is a protein that in humans is encoded by the NOC2L gene.
References
Further reading |
https://en.wikipedia.org/wiki/HAVCR1 | Hepatitis A virus cellular receptor 1 (HAVcr-1) also known as T-cell immunoglobulin and mucin domain 1 (TIM-1) is a protein that in humans is encoded by the HAVCR1 gene.
It is also known as KIM-1 Kidney Injury Molecule -1, which is a protein the most highly upregulated in injured kidneys by various types of insults. Its upregulation during renal injury has been found in the kidneys of the vertebrates such as Zebrafish and humans.
The hepatitis A virus cellular receptor 1 (HAVCR1/TIM-1), is a member of the TIM (T cell transmembrane, immunoglobulin, and mucin) gene family, which plays critical roles in regulating immune cell activity especially regarding the host response to viral infection. TIM-1 is also involved in allergic response, asthma, and transplant tolerance.
The TIM gene family was first cloned from the mouse model of asthma in 2001. Subsequently, it was demonstrated that members of the TIM gene family including TIM-1 participate in host immune response. The mouse TIM gene family contains eight members (TIM-1-8) while only three TIM genes (TIM-1, TIM-3, and TIM-4) have been identified in humans.
Structure and function
TIM genes belong to type I cell-surface glycoproteins, which include an N-terminal immunoglobulin (Ig)-like domain, a mucin domain with distinct length, a single transmembrane domain, and a C-terminal short cytoplasmic tail. The localization and functions of TIM genes are divergent between each member. TIM-1 is preferentially expressed on Th2 cel |
https://en.wikipedia.org/wiki/AKAP8L | A-kinase anchor protein 8-like is a protein that in humans is encoded by the AKAP8L gene.
Interactions
AKAP8L has been shown to interact with:
DHX9, and
Thymopoietin.
References
External links
Further reading
A-kinase-anchoring proteins |
https://en.wikipedia.org/wiki/VPS4A | Vacuolar protein sorting-associated protein 4A is a protein that in humans is encoded by the VPS4A gene.
Function
The protein encoded by this gene is a member of the AAA protein family (ATPases associated with diverse cellular activities), and is the homolog of the yeast Vps4 protein. In humans, two paralogs of the yeast protein have been identified. They share a high degree of amino acid sequence similarity with each other, and also with yeast Vps4 and mouse proteins. Functional studies indicate that both human paralogs associate with the endosomal compartments, and are involved in intracellular protein trafficking, similar to Vps4 protein in yeast. The gene encoding this paralog has been mapped to chromosome 16; the gene for the other resides on chromosome 18.
Interactions
VPS4A has been shown to interact with CHMP1A.
References
Further reading |
https://en.wikipedia.org/wiki/PIKFYVE | PIKfyve, a FYVE finger-containing phosphoinositide kinase, is an enzyme that in humans is encoded by the PIKFYVE gene.
Function
The principal enzymatic activity of PIKfyve is to phosphorylate PtdIns3P to PtdIns(3,5)P2. PIKfyve activity is responsible for the production of both PtdIns(3,5)P2 and phosphatidylinositol 5-phosphate (PtdIns5P). PIKfyve is a large protein, containing a number of functional domains and expressed in several spliced forms. The reported full-length mouse and human cDNA clones encode proteins of 2052 and 2098 amino acid residues, respectively. By directly binding membrane PtdIns(3)P, the FYVE finger domain of PIKfyve is essential in localizing the protein to the cytosolic leaflet of endosomes. Impaired PIKfyve enzymatic activity by dominant-interfering mutants, siRNA- mediated ablation or pharmacological inhibition causes lysosome enlargement and cytoplasmic vacuolation due to impaired PtdIns(3,5)P2 synthesis and impaired lysosome fission process and homeostasis. Thus, via PtdIns(3,5)P2 production, PIKfyve participates in several aspects of vesicular dynamics, thereby affecting a number of trafficking pathways that emanate from or traverse the endosomal system en route to the trans-Golgi network or later compartments along the endocytic pathway.
Medical significance
PIKfyve mutations affecting one of the two PIKFYVE alleles are found in 8 out of 10 families with Francois-Neetens corneal fleck dystrophy. Disruption of both PIKFYVE alleles in the mo |
https://en.wikipedia.org/wiki/RhoG | RhoG (Ras homology Growth-related) (or ARGH) is a small (~21 kDa) monomeric GTP-binding protein (G protein), and is an important component of many intracellular signalling pathways. It is a member of the Rac subfamily of the Rho family of small G proteins and is encoded by the gene RHOG.
Discovery
RhoG was first identified as a coding sequence upregulated in hamster lung fibroblasts upon stimulation with serum. Expression of RhoG in mammals is widespread and studies of its function have been carried out in fibroblasts, leukocytes, neuronal cells, endothelial cells and HeLa cells. RhoG belongs to the Rac subgroup and emerged as a consequence of retroposition in early vertebrates. RhoG shares a subset of common binding partners with Rac, Cdc42 and RhoU/V members but a major specificity is its inability to bind to CRIB domain proteins such as PAKs.
Function
Like most small G proteins RhoG is involved in a diverse set of cellular signalling mechanisms. In mammalian cells these include cell motility (through regulation of the actin cytoskeleton), gene transcription, endocytosis, neurite outgrowth, protection from anoikis and regulation of the neutrophil NADPH oxidase.
Regulation of RhoG activity
As with all small G proteins RhoG is able to signal to downstream effectors when bound to GTP (Guanosine triphosphate) and unable to signal when bound to GDP (Guanosine diphosphate).
Three classes of protein interact with RhoG to regulate GTP/GDP loading. The first are known as Guanine |
https://en.wikipedia.org/wiki/PHOX2A | Paired mesoderm homeobox protein 2A is a protein that in humans is encoded by the PHOX2A gene.
Function
The protein encoded by this gene contains a paired-like homeodomain most similar to that of the Drosophila aristaless gene product. This protein is expressed specifically in noradrenergic cell types. It regulates the expression of tyrosine hydroxylase and dopamine beta-hydroxylase, two catecholaminergic biosynthetic enzymes essential for the differentiation and maintenance of noradrenergic phenotype. Mutations in this gene have been associated with autosomal recessive congenital fibrosis of the extraocular muscles (CFEOM2).
Interactions
PHOX2A has been shown to interact with HAND2.
References
Further reading
External links
Engle Laboratory CFEOM page
GeneReviews/NCBI/NIH/UW entry on Congenital Fibrosis of the Extraocular Muscles
OMIM entries on Congenital Fibrosis of the Extraocular Muscles
Transcription factors |
https://en.wikipedia.org/wiki/GPS1 | COP9 signalosome complex subunit 1 is a protein that in humans is encoded by the GPS1 gene.
This gene is known to suppress G-protein and mitogen-activated signal transduction in mammalian cells. The encoded protein shares significant similarity with Arabidopsis FUS6, which is a regulator of light-mediated signal transduction in plant cells. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.
References
Further reading |
https://en.wikipedia.org/wiki/GPX2%20%28gene%29 | Glutathione peroxidase 2 is an enzyme that in humans is encoded by the GPX2 gene.
This gene is a member of the glutathione peroxidase family encoding a selenium-dependent glutathione peroxidase that is one of two isoenzymes responsible for the majority of the glutathione-dependent hydrogen peroxide-reducing activity in the epithelium of the gastrointestinal tract. Studies in knockout mice indicate that mRNA expression levels respond to luminal microflora, suggesting a role of the ileal glutathione peroxidases in preventing inflammation in the GI tract.
The antioxidant enzyme glutathione peroxidase 2 (Gpx2) is one out of eight known glutathione peroxidases (Gpx1-8) in humans. Mammalian Gpx1, GPx2 (this protein), Gpx3, and Gpx4 have been shown to be selenium-containing enzymes, whereas Gpx6 is a selenoprotein in humans with cysteine-containing homologues in rodents. In selenoproteins, the 21st amino acid selenocysteine is inserted in the nascent polypeptide chain during the process of translational recoding of the UGA stop codon.
References
Further reading
EC 1.11.1
Selenoproteins |
https://en.wikipedia.org/wiki/GSPT1 | Eukaryotic peptide chain release factor GTP-binding subunit ERF3A is an enzyme that in humans is encoded by the GSPT1 gene.
Interactions
GSPT1 has been shown to interact with BIRC2.
References
Further reading
External links |
https://en.wikipedia.org/wiki/GSTA4 | Glutathione S-transferase A4, also known as GSTA4, is an enzyme which in humans is encoded by the GSTA4 gene.
Function
Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase belonging to the alpha class. The alpha class genes, which are located in a cluster on chromosome 6, are highly related and encode enzymes with glutathione peroxidase activity that function in the detoxification of lipid peroxidation products.
GSTA4 shows very high activity with reactive carbonyl compounds such as alk-2-enals. GSTA4 is highly effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, an important product of peroxidative degradation of arachidonic acid and a commonly used biomarker for oxidative damage in tissue.
Clinical significance
Reactive electrophiles produced by oxidative metabolism have been linked to a number of degenerative diseases including Parkinson's disease, Alzheimer's disease, cataract formation, and atherosclerosis hence reduced expression of the GSTA4 enzyme may have pathophysiological consequences. The expression of this gene is decr |
https://en.wikipedia.org/wiki/HMGN2 | Non-histone chromosomal protein HMG-17 is a protein that in humans is encoded by the HMGN2 gene.
See also
High mobility group protein HMG14 and HMG17
HMGN1 (HMG-14)
References
Further reading |
https://en.wikipedia.org/wiki/HNRNPAB | Heterogeneous nuclear ribonucleoprotein A/B, also known as HNRNPAB, is a protein which in humans is encoded by the HNRNPAB gene. Although this gene is named HNRNPAB in reference to its first cloning as an RNA binding protein with similarity to HNRNP A and HNRNP B, it is not a member of the HNRNP A/B subfamily of HNRNPs, but groups together closely with HNRNPD/AUF1 and HNRNPDL.
Function
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are produced by RNA polymerase II and are components of the heterogeneous nuclear RNA (hnRNA) complexes. They are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene, which binds to one of the components of the multiprotein editosome complex, has two repeats of quasi-RRM (RNA recognition motif) domains that bind to RNAs. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.
Interactions
HNRNPAB has been shown to interact with TP63.
References
Further reading |
https://en.wikipedia.org/wiki/IFRD1 | Interferon-related developmental regulator 1 is a protein that in humans is encoded by the IFRD1 gene. The gene is expressed mostly in neutrophils, skeletal and cardiac muscle, the brain, and the pancreas.
The rat and the mouse homolog genes of interferon-related developmental regulator 1 gene (and their proteins) are also known with the name PC4 and Tis21, respectively.
IFRD1 is member of a gene family that comprises a second gene, IFRD2, also known as SKmc15.
Clinical significance
IFRD1 has been identified as a modifier gene for cystic fibrosis lung disease. In humans, neutrophil effector function is dependent on the type of IRFD1 polymorphism present in the individual. Human and mouse data both indicate that IFRD1 has a sizable impact on cystic fibrosis pathogenesis by regulating neutrophil effector function.
Inducer of muscle regeneration
IFRD1(also known as PC4 or Tis7, see above) participates to the process of skeletal muscle cell differentiation. In fact, inhibition of IFRD1 function in C2C12 myoblasts, by antisense IFRD1 cDNA transfection or microinjection of anti-IFRD1 antibodies, prevents their morphological and biochemical differentiation by inhibiting the expression of MyoD and myogenin, key master genes of muscle development. A role for IFRD1 in muscle differentiation has been observed also in vivo. Muscles from mice lacking IFRD1 display decreased protein and mRNA levels of MyoD, and myogenin, and after muscle crash damage in young mice there was a delay |
https://en.wikipedia.org/wiki/Interleukin%2011%20receptor%20alpha%20subunit | Interleukin 11 receptor, alpha subunit is a subunit of the interleukin 11 receptor. IL11RA is its human gene.
Interleukin 11 is a stromal cell-derived cytokine that belongs to a family of pleiotropic and redundant cytokines that use the gp130 transducing subunit in their high affinity receptors. This gene encodes the IL-11 receptor, which is a member of the hematopoietic cytokine receptor family. This particular receptor is very similar to ciliary neurotrophic factor, since both contain an extracellular region with a 2-domain structure composed of an immunoglobulin-like domain and a cytokine receptor-like domain. Alternative splicing has been observed at this locus and two variants, each encoding a distinct isoform, have been identified.
References
Further reading |
https://en.wikipedia.org/wiki/KCNK2 | Potassium channel subfamily K member 2, also known as TREK-1, is a protein that in humans is encoded by the KCNK2 gene.
This gene encodes K2P2.1, a lipid-gated ion channel belonging to the two-pore-domain background potassium channel protein family. This type of potassium channel is formed by two homodimers that create a channel that releases potassium out of the cell to control resting membrane potential. The channel is opened by anionic lipid, certain anesthetics, membrane stretching, intracellular acidosis, and heat. Three transcript variants encoding different isoforms have been found for this gene.
Function in neurons
TREK-1 is part of the subfamily of mechano-gated potassium channels that are present in mammalian neurons. They can be gated in both chemical and physical ways and can be opened via both physical stimuli and chemical stimuli. TREK-1 channels are found in a variety of tissues, but are particularly abundant in the brain and heart and are seen in various types of neurons. The C-terminal of TREK-1 channels plays a role in the mechanosensitivity of the channels.
In the neurons of the central nervous system, TREK-1 channels are important in physiological, pathophysiological, and pharmacological processes, including having a role in electrogenesis, ischemia, and anesthesia. TREK-1 has an important role in neuroprotection against epilepsy and brain and spinal cord ischemia and is being evaluated as a potential target for new developments of therapeutic age |
https://en.wikipedia.org/wiki/KIF22 | Kinesin-like protein KIF22 is a protein that in humans is encoded by the KIF22 gene.
The protein encoded by this gene is a member of kinesin-like protein family. This family of proteins are microtubule-dependent molecular motors that transport organelles within cells and move chromosomes during cell division. The C-terminal half of this protein has been shown to bind DNA. Studies with the Xenopus homolog suggests an essential role in metaphase chromosome alignment and maintenance.
Interactions
KIF22 has been shown to interact with SIAH1.
Clinical relevance
Mutations in this gene have been shown to cause developmental disorders such as Spondyloepimetaphyseal dysplasia with joint laxity.
References
Further reading |
https://en.wikipedia.org/wiki/Galectin-9 | Galectin-9 was first isolated from mouse embryonic kidney in 1997 as a 36 kDa beta-galactoside lectin protein. Human galectin-9 is encoded by the LGALS9 gene.
Function
The protein has N- and C- terminal carbohydrate-binding domains connected by a link peptide. Multiple alternatively spliced transcript variants have been found for this gene.
Galectin-9 is one of the most studied ligands for HAVCR2 (TIM-3) and is expressed on various tumor cells. However, it can also interact with other proteins (CLEC7A, CD137, CD40). For example, an interaction with CD40 on T-cells inhibits their proliferation and induces cell death.
Galectin-9 also has important cytoplasmic, intracellular functions and controls AMPK in response to lysosomal damage that can occur upon exposure to endogenous and exogenous membrane damaging agents such as crystalline silica, cholesterol crystals, microbial toxins, proteopathic aggregates such as tau fibrils and amyloids, and signaling pathways inducing lysosomal permeabilization such as those initiated by TRAIL. Mild lysosomal damage, such as that caused by the anti-diabetes drug metformin may contribute to the therapeutic action of metformin by activating AMPK. The mechanism of how Galectin-9 activates AMPK involves recognition of exposed lysosomal lumenal glycoproteins such as LAMP1, LAMP2, SCRAB2, TMEM192, etc., repulsion of deubiquitinating enzyme USP9X, increased K63 ubiquitination of TAK1 (MAP3K7) kinase, which in turn phopshorylates AMPK and activ |
https://en.wikipedia.org/wiki/MAGOH | Protein mago nashi homolog is a protein that in humans is encoded by the MAGOH gene.
Drosophila that have mutations in their mago nashi (grandchildless) gene produce progeny with defects in germplasm assembly and germline development. This gene encodes the mammalian mago nashi homolog. In mammals, mRNA expression is not limited to the germ plasm, but is expressed ubiquitously in adult tissues and can be induced by serum stimulation of quiescent fibroblasts.
Interactions
MAGOH has been shown to interact with RBM8A and NXF1. In Drosophila melanogaster, Mago Nashi and Tsunagi/Y14 (core components of the exon junction complex) form a complex with a novel zinc finger protein, Ranshi, that has a role in oocyte differentiation.
References
Further reading |
https://en.wikipedia.org/wiki/MAL%20%28gene%29 | Myelin and lymphocyte protein is a protein that in humans is encoded by the MAL gene.
Function
The protein encoded by this gene is a highly hydrophobic integral membrane protein belonging to the MAL family of proteolipids. The protein has been localized to the endoplasmic reticulum of T-cells and is a candidate linker protein in T-cell signal transduction. In addition, this proteolipid is localized in compact myelin of cells in the nervous system and has been implicated in myelin biogenesis and/or function. The protein plays a role in the formation, stabilization and maintenance of glycosphingolipid-enriched membrane microdomains. Alternative splicing produces four transcript variants which vary from each other by the presence or absence of alternatively spliced exons 2 and 3. The MAL protein is also thought to interact with the protein encoded by LSMEM1 based on two-hybrid screening.
References
Further reading |
https://en.wikipedia.org/wiki/MCF2 | The DBL proto-oncogene is a protein that in humans is encoded by the MCF2 gene.
The commonly-used name DBL is derived from “diffuse B-cell lymphoma”, the cancer type where this gene was first identified as an oncogene, while the name MCF2 name derives from “MCF.2 cell line-derived transforming sequence”.
DBL is the founding member of a large family of guanine nucleotide exchange factors that share a common DBL-homology (DH) domain), so DBL is also named as a member of this RhoGEF family as ARHGEF21. DH domains function to activate small GTPases of the Rho family by facilitating release of GDP from an inactive Rho GTPase and binding of GTP to activate it. In particular, DBL activates the Rho family member Cdc42.
Gene recombinations that result in the loss of N-terminal regions produce MCF2 variants with oncogenic activity.[supplied by OMIM]
References
Further reading |
https://en.wikipedia.org/wiki/MAP3K4 | Mitogen-activated protein kinase kinase kinase 4 is an enzyme that in humans is encoded by the MAP3K4 gene.
The central core of each mitogen-activated protein kinase (MAPK) pathway is a conserved cascade of 3 protein kinases: an activated MAPK kinase kinase (MAPKKK) phosphorylates and activates a specific MAPK kinase (MAPKK), which then activates a specific MAPK. While the ERK MAPKs are activated by mitogenic stimulation, the CSBP2 (p38α) and JNK MAPKs are activated by environmental stresses such as osmotic shock, UV irradiation, wound stress, and inflammatory factors. This gene encodes a MAPKKK, the MEKK4 protein, also called MTK1. This protein contains a protein kinase catalytic domain at the C terminus. The N-terminal nonkinase domain may contain a regulatory domain. Expression of MEKK4 in mammalian cells activated the CSBP2 (p38α) and JNK MAPK pathways, but not the ERK pathway. In vitro kinase studies indicated that recombinant MEKK4 can specifically phosphorylate and activate PRKMK6 (MKK6) and SERK1 (MKK4), MAPKKs that activate CSBP2 (p38α) and JNK, respectively but cannot phosphorylate PRKMK1 (MKK1), an MAPKK that activates ERKs. MEKK4 is a major mediator of environmental stresses that activate the p38 MAPK pathway, and a minor mediator of the JNK pathway. Two alternatively spliced transcripts encoding distinct isoforms have been described.
Interactions
MAP3K4 has been shown to interact with GADD45G, GADD45B and GADD45A.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/MAP3K10 | Mitogen-activated protein kinase kinase kinase 10 is an enzyme that in humans is encoded by the MAP3K10 gene.
Function
The protein encoded by this gene is a member of the serine/threonine kinase family. This kinase has been shown to activate MAPK8/JNK and MKK4/SEK1, and this kinase itself can be phosphorylated, and thus activated by JNK kinases. This kinase functions preferentially on the JNK signaling pathway, and is reported to be involved in nerve growth factor (NGF) induced neuronal apoptosis.
Interactions
MAP3K10 has been shown to interact with:
CDC42,
Huntingtin,
KIF3A,
MAPK8IP1,
MAPK8IP2, and
NEUROD1.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/Tate%27s%20algorithm | In the theory of elliptic curves, Tate's algorithm takes as input an integral model of an elliptic curve E over , or more generally an algebraic number field, and a prime or prime ideal p. It returns the exponent fp of p in the conductor of E, the type of reduction at p, the local index
where is the group of -points
whose reduction mod p is a non-singular point. Also, the algorithm determines whether or not the given integral model is minimal at p, and, if not, returns an integral model with integral coefficients for which the valuation at p of the discriminant is minimal.
Tate's algorithm also gives the structure of the singular fibers given by the Kodaira symbol or Néron symbol, for which, see elliptic surfaces: in turn this determines the exponent fp of the conductor E.
Tate's algorithm can be greatly simplified if the characteristic of the residue class field is not 2 or 3; in this case the type and c and f can be read off from the valuations of j and Δ (defined below).
Tate's algorithm was introduced by as an improvement of the description of the Néron model of an elliptic curve by .
Notation
Assume that all the coefficients of the equation of the curve lie in a complete discrete valuation ring R with perfect residue field K and maximal ideal generated by a prime π.
The elliptic curve is given by the equation
Define:
the p-adic valuation of in , that is, exponent of in prime factorization of , or infinity if
The algorithm
Step 1: If π does not divide Δ |
https://en.wikipedia.org/wiki/MTCP1 | Protein p13 MTCP-1 is a protein that in humans is encoded by the MTCP1 gene.
Function
This gene was identified by involvement in some t(X;14) translocations associated with mature T-cell proliferations. The gene has two ORFs that encode two different proteins. The upstream ORF encodes a 13kDa protein that is a member of the TCL1 family; this protein may be involved in leukemogenesis. The downstream ORF encodes an 8kDa protein that localizes to mitochondria. Alternative splicing results in multiple transcript variants.
Interactions
MTCP1 has been shown to interact with AKT1.
References
Further reading |
https://en.wikipedia.org/wiki/Mucin%206 | Mucin 6, oligomeric mucus/gel-forming, also known as MUC6, is a human gene encoding a protein of the same name. MUC6, along with MUC2, MUC5AC, and MUC5B, is located within the 11p15 chromosomal locus of chromosome 11. MUC6, along with MUC1, is expressed in normal pancreases.
References
06 |
https://en.wikipedia.org/wiki/FHOD1 | FH1/FH2 domain-containing protein 1 is a protein that in humans is encoded by the FHOD1 gene.
This gene encodes a protein which is a member of the formin/diaphanous family of proteins. The gene is ubiquitously expressed but is found in abundance in the spleen. The encoded protein has sequence homology to diaphanous and formin proteins within the Formin Homology (FH)1 and FH2 domains. It also contains a coiled-coil domain, a collagen-like domain, two nuclear localization signals, and several potential PKC and PKA phosphorylation sites. It is a predominantly cytoplasmic protein and is expressed in a variety of human cell lines.
Interactions
FHOD1 has been shown to interact with RAC1.
References
Further reading |
https://en.wikipedia.org/wiki/EEF2K | Eukaryotic elongation factor-2 kinase (eEF-2 kinase or eEF-2K), also known as calmodulin-dependent protein kinase III (CAMKIII) and calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase, is an enzyme that in humans is encoded by the EEF2K gene.
Function
eEF-2 kinase is a highly conserved protein kinase in the calmodulin-mediated signaling pathway that links multiple up-stream signals to the regulation of protein synthesis. It phosphorylates eukaryotic elongation factor 2 (EEF2) and thus inhibits the EEF2 function.
Activation
The activity of eEF-2K is dependent on calcium and calmodulin. Activation of eEF-2K proceeds by a sequential two-step mechanism. First, calcium-calmodulin binds with high affinity to activate the kinase domain, triggering rapid autophosphorylation of Thr-348. In the second step, autophosphorylation of Thr-348 leads to a conformational change in the kinase likely supported by the binding of phospho-Thr-348 to an allosteric phosphate binding pocket in the kinase domain. This increases the activity of eEF-2K against its substrate, elongation factor 2.
eEF-2K can gain calcium-independent activity through autophosphorylation of Ser-500. However, calmodulin must remain bound to the enzyme for its activity to be sustained.
Clinical significance
The activity of this kinase is increased in many cancers and may be a valid target for anti-cancer treatment.
It is also suggested that eEF-2K may play a role the rapid anti-depressant effects of k |
https://en.wikipedia.org/wiki/A1CF | APOBEC1 complementation factor is a protein that in humans is encoded by the A1CF gene.
Gene
Alternative splicing occurs at this locus and three full-length transcript variants, encoding three distinct isoforms, have been described. Additional splicing has been observed but the full-length nature of these variants has not been determined.
Function
Mammalian apolipoprotein B mRNA undergoes site-specific C to U deamination, which is mediated by a multi-component enzyme complex containing a minimal core composed of APOBEC1 and a complementation factor encoded by this gene. The gene product has three non-identical RNA recognition motifs and belongs to the hnRNP R family of RNA-binding proteins. It has been proposed that this complementation factor functions as an RNA-binding subunit and docks APOBEC1 to deaminate the upstream cytidine. Studies suggest that the protein may also be involved in other RNA editing or RNA processing events.
Its deletion results in lethality in mice.
Interactions
A1CF has been shown to interact with APOBEC1, CUGBP2, and SYNCRIP.
References
External links
Further reading
Human proteins |
https://en.wikipedia.org/wiki/SUMO4 | Small ubiquitin-related modifier 4 is a protein that in humans is encoded by the SUMO4 gene.
Function
This gene is a member of the SUMO gene family. This family of genes encode small ubiquitin-related modifiers that are attached to proteins and control the target proteins' subcellular localization, stability, or activity. The protein described in this record is located in the cytoplasm and specifically modifies IKBA, leading to negative regulation of NF-kappa-B-dependent transcription of the IL12B gene. A specific polymorphism in this SUMO gene, which leads to the M55V substitution, has been associated with type I diabetes. The RefSeq contains this polymorphism.
Interactions
SUMO4 has been shown to interact with IκBα.
References
Further reading |
https://en.wikipedia.org/wiki/ATP2A3 | Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 is an enzyme that in humans is encoded by the ATP2A3 gene.
This gene encodes one of the SERCA Ca2+-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of cells. SERCA3 expression was originally described as non-muscular, but was recently observed in cardiomyocyte. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in calcium sequestration associated with muscular excitation and contraction. Alternative splicing results in 6 transcript variants encoding different isoforms named SERCA3a to SERCA3f.
Cancer
ATP2A3 gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. For this reason, ATP2A3 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.
References
External links
Further reading |
https://en.wikipedia.org/wiki/ATP5PF | ATP synthase-coupling factor 6, mitochondrial is an enzyme subunit that in humans is encoded by the ATP5PF gene.
Function
Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, FO, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The FO seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the F6 subunit of the FO complex, required for F1 and FO interactions. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.
The F6 subunit is part of the peripheral stalk that links the F1 and FO complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In mitochondria, the peripheral stalk is composed of one copy each of subunits OSCP (oligomycin sensitivity conferral protein), F6, b and d. There is no homologue of subunit F6 in bacterial or chloroplast F-ATPase, whose peripheral stalks are composed of one copy of the delta subunit (homologous to OSCP), |
https://en.wikipedia.org/wiki/ATP6V1B2 | V-type proton ATPase subunit B, brain isoform is an enzyme that in humans is encoded by the ATP6V1B2 gene.
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. The protein encoded by this gene is one of two V1 domain B subunit isoforms and is the only B isoform highly expressed in osteoclasts.
In melanocytic cells ATP6V1B2 gene expression may be regulated by MITF.
References
External links
Further reading |
https://en.wikipedia.org/wiki/ATP6AP1 | The human gene ATP6AP1 encodes the S1 subunit of the enzyme V-type proton ATPase.
This gene encodes a component of a multisubunit enzyme (1 mDa MW) that mediates acidification of eukaryotic intracellular organelles. Vacuolar ATPase (V-ATPase) is composed of a cytosolic, V1, (site of the ATP catalytic site) and a transmembrane, V0, domain. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, and receptor-mediated endocytosis. The encoded protein of this gene is approximately 45 kD and may assist in the V-ATPase-mediated acidification of neuroendocrine secretory granules.
References
External links
Further reading |
https://en.wikipedia.org/wiki/Mucin%207 | Mucin-7 is a protein that in humans is encoded by the MUC7 gene. In animals, the MUC7 gene is found in most placental mammals, but not marsupials.
Human variations
Humans carry either a five or six tandem repeat version of the gene. In other primates, the number of repeats found is 4-5 for gorillas, 5 for chimpanzees, 6-7 for orangutans, 8-10 for macaques, 10-11 for baboons and 11-12 for green monkeys.
References
Further reading
07 |
https://en.wikipedia.org/wiki/TRIM37 | Tripartite motif-containing protein 37 is an E3 ubiquitin ligase in humans that is encoded by the TRIM37 gene.
Function
This gene encodes a member of the tripartite motif (TRIM) family, whose members are involved in diverse cellular functions such as developmental patterning and oncogenesis. The TRIM motif includes zinc-binding domains, a RING finger region, a B-box motif and a coiled-coil domain. The RING finger and B-box domains chelate zinc and might be involved in protein–protein and/or protein–nucleic acid interactions. The gene mutations are associated with mulibrey (muscle-liver-brain-eye) nanism, an autosomal recessive disorder that involves several tissues of mesodermal origin. Alternatively spliced transcript variants encoding the same protein have been identified. It is responsible for the mono-ubiquitination of histone H2A at lysine 119, a modification commonly associated with transcriptional repression.
Role in breast cancer
The 17q23 chromosomal region in which the TRIM37 gene is located has been shown to be amplified in up to 40% of breast cancers. The TRIM37 protein is thought to play a role in breast cancer oncogenesis by ubiquitinating histone H2A in regions occupied by tumor-suppressing genes. This repression of tumor-suppressing genes increases the likelihood that a tumor will occur or that an existing tumor will be more aggressive.
Interactions
TRIM37 has been shown to interact with PRC1. TRIM37 has also been shown to interact with PRC2 to alter i |
https://en.wikipedia.org/wiki/NDN%20%28gene%29 | Necdin is a protein that in humans is encoded by the NDN gene.
Function
This intronless gene is located in the Prader-Willi syndrome (PWS) deletion region. It is an imprinted gene and is expressed exclusively from the paternal allele. Studies in mice suggest that the protein encoded by this gene may suppress growth in postmitotic neurons.
Necdin is used to stimulate growth regulation and DNA-dependent transcription regulation.
Interactions
NDN (gene) has been shown to interact with:
E2F1,
HNRNPU,
IL1A,
Low affinity nerve growth factor receptor,
NUCB2, and
P53
References
Further reading
Human proteins |
https://en.wikipedia.org/wiki/NRCAM | Neuronal cell adhesion molecule is a protein that in humans is encoded by the NRCAM gene.
Cell adhesion molecules (CAMs) are members of the immunoglobulin superfamily. This gene encodes a neuronal cell adhesion molecule with multiple immunoglobulin-like C2-type domains and fibronectin type-III domains. This ankyrin-binding protein is involved in neuron-neuron adhesion and promotes directional signaling during axonal cone growth. This gene is also expressed in non-neural tissues and may play a general role in cell-cell communication via signaling from its intracellular domain to the actin cytoskeleton during directional cell migration. Allelic variants of this gene have been associated with autism and addiction vulnerability. Alternative splicing results in multiple transcript variants encoding different isoforms.
References
Further reading |
https://en.wikipedia.org/wiki/Discoidin%20domain-containing%20receptor%202 | Discoidin domain-containing receptor 2, also known as CD167b (cluster of differentiation 167b), is a protein that in humans is encoded by the DDR2 gene. Discoidin domain-containing receptor 2 is a receptor tyrosine kinase (RTK).
Function
RTKs play a key role in the communication of cells with their microenvironment. These molecules are involved in the regulation of cell growth, differentiation, and metabolism. In several cases the biochemical mechanism by which RTKs transduce signals across the membrane has been shown to be ligand induced receptor oligomerization and subsequent intracellular phosphorylation. In the case of DDR2, the ligand is collagen which binds to its extracellular discoidin domain. This autophosphorylation leads to phosphorylation of cytosolic targets as well as association with other molecules, which are involved in pleiotropic effects of signal transduction. DDR2 has been associated with a number of diseases including fibrosis and cancer.
Structure
RTKs have a tripartite structure with extracellular, transmembrane, and cytoplasmic regions. This gene encodes a member of a novel subclass of RTKs and contains a distinct extracellular region encompassing a factor VIII-like domain.
Gene
Alternative splicing in the 5' UTR of the DDR2 gene results in multiple transcript variants encoding the same protein.
Interactions
DDR2 (gene) has been shown to interact with SHC1 and phosphorylate Shp2. DDR2 also interacts with Integrin α1β1 and α2β1 by promoti |
https://en.wikipedia.org/wiki/Nucleoporin%2088 | Nucleoporin 88 (Nup88) is a protein that in humans is encoded by the NUP88 gene.
Function
The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins, a family of 50 to 100 proteins, are the main components of the nuclear pore complex in eukaryotic cells. The protein encoded by this gene belongs to the nucleoporin family and is associated with the oncogenic nucleoporin CAN/Nup214 in a dynamic subcomplex. This protein is also overexpressed in a large number of malignant neoplasms and precancerous dysplasias.
Interactions
NUP88 has been shown to interact with NUP98.
References
Further reading
Nuclear pore complex |
https://en.wikipedia.org/wiki/Osteoglycin | Osteoglycin (also called mimecan), encoded by the OGN gene, is a human protein.
This gene encodes a protein which induces ectopic bone formation in conjunction with transforming growth factor beta. This protein is a small keratan sulfate proteoglycan which contains tandem leucine-rich repeats (LRR). The gene expresses three transcript variants.
The level of expression of this gene has been correlated with enlarged hearts and more specifically left ventricular hypertrophy.
References
Further reading
Proteoglycans
Extracellular matrix proteins |
https://en.wikipedia.org/wiki/PCSK6 | Proprotein convertase subtilisin/kexin type 6 is an protease that in humans is encoded by the PCSK6 gene which is located in chromosome 15. Pcsk6 is a calcium-dependent serine endoprotease that catalyzes the post-translational modification of precursor proteins from its ‘latent’ form to the cleaved ‘active’ form. Active Pcsk6 has been reported to process substrates such as transforming growth factor β, pro-albumin, von Willebrand factor, and corin. Clinically, Pcsk6 is suggested to play a role in left/right asymmetry, structural asymmetry of the brain, handedness, tumor progression, hemostasis, and cardiovascular diseases.
Function
The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine endoprotease that can cleave precursor protein at their paired basic amino acid processing sites. Some of its substrates are - transforming growth factor beta related proteins, pro-albumin, von Willebrand factor, and corin. Alternatively spliced transcript variants encoding different isoforms have been identified.
Clinical significance
During development: Throughout development, the spatial and temporal expression of pcsk6 regulates embryogenesis by activating TGFβ related differentiation factors, which include BMP and Nodal. Elevated levels of Pcsk6 was detected in ma |
https://en.wikipedia.org/wiki/Phosducin-like | Phosducin-like protein is a protein that in humans is encoded by the PDCL gene.
Phosducin-like protein is a putative modulator of heterotrimeric G proteins. The protein shares extensive amino acid sequence homology with phosducin, a phosphoprotein expressed in the retina and pineal gland. Both phosducin-like protein and phosphoducin have been shown to regulate G-protein signaling by binding to the beta-gamma subunits of G proteins.
References
Further reading |
https://en.wikipedia.org/wiki/PCMT1 | Protein-L-isoaspartate(D-aspartate) O-methyltransferase is an enzyme that in humans is encoded by the PCMT1 gene.
Three classes of protein carboxyl methyltransferases, distinguished by their methyl-acceptor substrate specificity, have been found in prokaryotic and eukaryotic cells. The type II enzyme catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the free carboxyl groups of D-aspartyl and L-isoaspartyl residues. These methyl-accepting residues result from the spontaneous deamidation, isomerization, and racemization of normal L-aspartyl and L-asparaginyl residues and represent sites of covalent damage to aging proteins PCMT1 (EC 2.1.1.77) is a protein repair enzyme that initiates the conversion of abnormal D-aspartyl and L-isoaspartyl residues to the normal L-aspartyl form.[supplied by OMIM]
References
Further reading |
https://en.wikipedia.org/wiki/PFDN1 | Prefoldin subunit 1 is a protein that in humans is encoded by the PFDN1 gene.
This gene encodes a member of the prefoldin beta subunit family. The encoded protein is one of six subunits of prefoldin, a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thereby allowing them to fold correctly. The complex, consisting of two alpha and four beta subunits, forms a double beta barrel assembly with six protruding coiled-coils.
References
Further reading |
https://en.wikipedia.org/wiki/Plakophilin-2 | Plakophilin-2 is a protein that in humans is encoded by the PKP2 gene. Plakophilin 2 is expressed in skin and cardiac muscle, where it functions to link cadherins to intermediate filaments in the cytoskeleton. In cardiac muscle, plakophilin-2 is found in desmosome structures located within intercalated discs. Mutations in PKP2 have been shown to be causal in arrhythmogenic right ventricular cardiomyopathy.
Structure
Two splice variants of the PKP2 gene have been identified. The first has a molecular weight of 97.4 kDa (881 amino acids) and the second of molecular weight of 92.7 kDa (837 amino acids). A processed pseudogene with high similarity to this locus has been mapped to chromosome 12p13.
Plakophilin-2 is a member of the armadillo repeat and plakophilin protein family. Plakophilin proteins contain nine central, conserved armadillo repeat domains flanked by N-terminal and C-terminal domains. Alternately spliced transcripts encoding protein isoforms have been identified.
Plakophilin 2 localizes to cell desmosomes and nuclei and binds plakoglobin, desmoplakin, and the desmosomal cadherins via N-terminal head domain.
Function
Plakophilin 2 functions to link cadherins to intermediate filaments in the cytoskeleton. In cardiomyocytes, plakophilin-2 is found at desmosome structures within intercalated discs, which link adjacent sarcolemmal membranes together. The desmosomal protein, desmoplakin, is the core constituent of the plaque which anchors intermediate filaments to t |
https://en.wikipedia.org/wiki/POU3F2 | POU domain, class 3, transcription factor 2 is a protein that in humans is encoded by the POU3F2 gene.
Function
N-Oct-3 is a protein belonging to a large family of transcription factors that bind to the octameric DNA sequence ATGCAAAT. Most of these proteins share a highly homologous region, referred to as the POU domain, which occurs in several mammalian transcription factors, including the octamer-binding proteins Oct1 (POU2F1; MIM 164175) and Oct2 (POU2F2; MIM 164176), and the pituitary protein Pit1 (PIT1; MIM 173110).
Class III POU genes are expressed predominantly in the CNS. It is likely that CNS-specific transcription factors such as these play an important role in mammalian neurogenesis by regulating their diverse patterns of gene expression.
Disease linkage
The POU3F2 protein associates with the Bipolar disorder. It is involved in the neocortex development in mice, and is linked to a single nucleotide polymorphism, Rs1906252, that is associated with a cognitive phenotype: processing information speed.
Chromosome 6q16.1 deletions resulting in loss of one copy of POU3F2 have been shown to cause a human syndrome of susceptibility to obesity and variable levels of developmental delay and Intellectual Disability.
Interactions
POU3F2 has been shown to interact with PQBP1.
See also
Octamer transcription factor
References
Further reading
External links
POU-domain proteins |
https://en.wikipedia.org/wiki/POU4F1 | POU domain, class 4, transcription factor 1 (POU4F1) also known as brain-specific homeobox/POU domain protein 3A (BRN3A), homeobox/POU domain protein RDC-1 or Oct-T1 is a protein that in humans is encoded by the POU4F1 gene.
BRN3A (POU4F1) is a class IV POU domain-containing transcription factor highly expressed in the developing peripheral sensory nervous system (dorsal root ganglia, trigeminal ganglion, and hindbrain sensory ganglia), certain regions of the central nervous system, retinal neurons called ganglion cells, and in cells of the B- and T-lymphocytic lineages.
Discovery
Brn3a was initially discovered in mice based on homology to the prototypal POU transcription factors Pit1 (Pituitary-specific positive transcription factor 1, Pou1f1), Oct1 (Pou2f1), and the Caenorhabditis elegans factor Unc86, and named Brn3. When multiple members of the Brn3 gene class were discovered, it was renamed Brn3.0 and Brn3a by different groups of researchers. Subsequently, the gene was systematically renamed Pou4f1 in mice and POU4F1 in humans. The protein product is still frequently referred to as Brn3a.
Function
In addition to sensory neurons, in rodents and birds (and presumably humans) Brn3a is expressed in multiple sites in the central nervous system, including the spinal cord, midbrain superior colliculus, red nucleus, nucleus ambiguus, inferior olivary nucleus, habenula, and retina.
Mice with null mutations ("knockouts") in Brn3a die at birth, due to developmental defects |
https://en.wikipedia.org/wiki/PPP1R2 | Protein phosphatase inhibitor 2 is an enzyme that in humans is encoded by the PPP1R2 gene.
Interactions
PPP1R2 has been shown to interact with LMTK2 and PPP1R9B.
References
Further reading |
https://en.wikipedia.org/wiki/ATP6V0A4 | V-type proton ATPase 116 kDa subunit a isoform 4 is an enzyme that in humans is encoded by the ATP6V0A4 gene.
Function
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent 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. This gene is one of four genes in man and mouse that encode different isoforms of the a subunit. Alternatively spliced transcript variants encoding the same protein have been described. Mutations in this gene are associated with renal tubular acidosis associated with preserved hearing.
Interactions
ATP6V0A4 has been shown to interact with PFKM.
References
External links
Further reading |
https://en.wikipedia.org/wiki/SNX9 | Sorting nexin-9 is a protein that in humans is encoded by the SNX9 gene.
This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This protein does not contain a coiled coil region, like some family members, but does contain an SH3 domain near its N-terminus. This protein interacts with the cytoplasmic domains of the precursor but not the processed forms of a disintegrin and metalloprotease domain 9 and 15. This protein binds the beta-appendage domain of adaptor protein 2 and may function to assist adaptor protein 2 in its role at the plasma membrane. This protein interacts with activated Cdc42-associated kinase-2 to regulate the degradation of epidermal growth factor receptor protein.
Interactions
SNX9 has been shown to interact with ADAM9, DNM2 and ADAM15.
References
Further reading |
https://en.wikipedia.org/wiki/CPSF2 | Cleavage and polyadenylation specificity factor subunit 2 is a protein that in humans is encoded by the CPSF2 gene. This protein is a subunit of the cleavage and polyadenylation specificity factor (CPSF) complex which plays a key role in pre-mRNA 3' end processing and polyadenylation. The CPSF2 protein connects the two subunits of the complex, mCF and mPSF. Its structure contributes both to the stability of the subunits interaction and to the flexibility of the complex necessary for function. This protein has been identified as an essential subunit of the complex as certain mutations in the region inhibit CPSF complex formation.
References
External links
Further reading |
https://en.wikipedia.org/wiki/GDAP1 | Ganglioside-induced differentiation-associated protein 1 is a type of protein that in humans is encoded by the GDAP1 gene.
This gene encodes a member of the ganglioside-induced differentiation-associated protein family, which may play a role in a signal transduction pathway during neuronal development. Mutations in this gene have been associated with various forms of Charcot-Marie-Tooth Disease and neuropathy. Two transcript variants encoding different isoforms have been identified for this gene.
References
Further reading
External links
In
In
In |
https://en.wikipedia.org/wiki/UGT1A4 | UDP-glucuronosyltransferase 1-4 is an enzyme that in humans is encoded by the UGT1A4 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. This enzyme has some glucuronidase activity towards bilirubin, although it is more active on amines, steroids, and sapogenins.
It is the main enzyme responsible for glucuronidation of the anticonvulsant lamotrigine.
References
Further reading |
https://en.wikipedia.org/wiki/PBK%20%28gene%29 | Lymphokine-activated killer T-cell-originated protein kinase is an enzyme that in humans is encoded by the PBK gene.
The protein encoded by this gene is a serine/threonine kinase related to the dual specific mitogen-activated protein kinase kinase (MAPKK) family. Evidence suggests that mitotic phosphorylation is required for its catalytic activity. This mitotic kinase may be involved in the activation of lymphoid cells and support testicular functions, with a suggested role in the process of spermatogenesis.
References
Further reading
External links |
https://en.wikipedia.org/wiki/PSPH | Phosphoserine phosphatase is an enzyme that in humans is encoded by the PSPH gene.
Function
The protein encoded by this gene belongs to a subfamily of the phosphotransferases. This encoded enzyme is responsible for the third and last step in L-serine formation. It catalyzes magnesium-dependent hydrolysis of L-phosphoserine and is also involved in an exchange reaction between L-serine and L-phosphoserine. Deficiency of this protein is thought to be linked to Williams syndrome.
Clinical significance
Homozygous or compound heterozygous mutations in PSPH cause Neu–Laxova syndrome and Phosphoserine phosphatase deficiency.
Model organisms
Model organisms have been used in the study of PSPH function. A conditional knockout mouse line called Psphtm1a(EUCOMM)Hmgu was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed: - In-depth immunological phenotyping
References
Further reading
External links |
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