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https://en.wikipedia.org/wiki/CAMK1 | Calcium/calmodulin-dependent protein kinase type 1 is an enzyme that in humans is encoded by the CAMK1 gene.
Calcium/calmodulin-dependent protein kinase I is expressed in many tissues and is a component of a calmodulin-dependent protein kinase cascade. Calcium/calmodulin directly activates calcium/calmodulin-dependent protein kinase I by binding to the enzyme and indirectly promotes the phosphorylation and synergistic activation of the enzyme by calcium/calmodulin-dependent protein kinase I kinase.
References
Further reading
External links
EC 2.7.11 |
https://en.wikipedia.org/wiki/Decoy%20receptor%203 | Decoy receptor 3 (Dcr3), also known as tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), TR6 and M68, is a soluble protein of the tumor necrosis factor receptor superfamily which inhibits Fas ligand-induced apoptosis.
Discovery
Dcr3 was identified in 1998 by the search of genes with homology to the TNFR gene superfamily in expressed sequence tag (EST) database.
Structure
The open reading frame of TNFRSF6B encodes 300 amino acids with a 29-residue signal sequence and four tandem cystein-rich repeats. Two transcript variants encoding the same isoform, but differing in the 5' UTR, have been observed for this gene. Unlike most of the other members of TNFR superfamily, TNFRSF6 is a soluble protein which contains no transmembrane domain.
Function
This gene belongs to the tumor necrosis factor receptor superfamily. It acts as a decoy receptor that competes with death receptors for ligand binding. The encoded protein is postulated to play a regulatory role in suppressing FasL- and LIGHT-mediated cell death and T cell activation as well as to induce angiogenesis via neutralization of TL1A. Overexpression of this gene has been noted in various tumors e.g. gastrointestinal tract tumors, and it is located in a gene-rich cluster on chromosome 20, with other potentially tumor-related genes.
Interactions
TNFRSF6B has been shown to interact with:
TNFSF14
Fas ligand.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Autoimmune Lymphoproli |
https://en.wikipedia.org/wiki/Decoy%20receptor%201 | Decoy receptor 1 (DCR1), also known as TRAIL receptor 3 (TRAILR3) and tumor necrosis factor receptor superfamily member 10C (TNFRSF10C), is a human cell surface receptor of the TNF-receptor superfamily.
Function
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contains an extracellular TRAIL-binding domain and a transmembrane domain, but no cytoplasmic death domain. This receptor is not capable of inducing apoptosis, and is thought to function as an antagonistic receptor that protects cells from TRAIL-induced apoptosis. This gene was found to be a p53-regulated DNA damage-inducible gene. The expression of this gene was detected in many normal tissues but not in most cancer cell lines, which may explain the specific sensitivity of cancer cells to the apoptosis-inducing activity of TRAIL.
References
Further reading
Clusters of differentiation
TNF receptor family |
https://en.wikipedia.org/wiki/Nucleolar%20phosphoprotein%20p130 | Nucleolar phosphoprotein p130 is a protein that in humans is encoded by the NOLC1 gene.
Interactions
Nucleolar phosphoprotein p130 has been shown to interact with coilin and CEBPB.
References
Further reading |
https://en.wikipedia.org/wiki/FLOT1 | Flotillin-1 is a protein that in humans is encoded by the FLOT1 gene.
Caveolae are small domains on the inner cell membrane involved in vesicular trafficking and signal transduction. FLOT1 encodes a caveolae-associated, integral membrane protein. The function of flotillin 1 has not been determined.
Interactions
FLOT1 has been shown to interact with SORBS1.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Perilipin-3 | Mannose-6-phosphate receptor binding protein 1 (M6PRBP1) is a protein which in humans is encoded by the M6PRBP1 gene. Its gene product, as well as the gene itself, is commonly known as TIP47.
Function
Mannose 6-phosphate receptors (MPRs) deliver lysosomal hydrolase from the Golgi to endosomes and then return to the Golgi complex. The protein encoded by this gene interacts with the cytoplasmic domains of both cation-independent and cation-dependent MPRs, and is required for endosome-to-Golgi transport. This protein also binds directly to the GTPase RAB9 (RAB9A), a member of the RAS oncogene family. The interaction with RAB9 has been shown to increase the affinity of this protein for its cargo.
The mannose-6-phosphate receptor-binding properties of TIP47 are disputed, despite the designation of M6PRBP1 as TIP47's gene symbol. TIP47 protein is most commonly described in the scientific literature as a coat protein for lipid droplets.
TIP47 belongs to the peripilin protein family and shares significant homology with the other genes of this family, including perilipin and adipophilin.
Interactions
M6PRBP1 has been shown to interact with both Mannose 6-phosphate receptors.
References
Further reading
External links |
https://en.wikipedia.org/wiki/SF3A1 | Splicing factor 3 subunit 1 is a protein that in humans is encoded by the SF3A1 gene.
This gene encodes subunit 1 of the splicing factor 3a protein complex. The splicing factor 3a heterotrimer includes subunits 1, 2 and 3 and is necessary for the in vitro conversion of 15S U2 snRNP into an active 17S particle that performs pre-mRNA splicing. Subunit 1 belongs to the SURP protein family; named for the SURP (also called SWAP or Suppressor-of-White-APricot) motifs that are thought to mediate RNA binding. Subunit 1 has tandemly repeated SURP motifs in its amino-terminal half while its carboxy-terminal half contains a proline-rich region and a ubiquitin-like domain. Binding studies with truncated subunit 1 derivatives demonstrated that the two SURP motifs are necessary for binding to subunit 3 while contacts with subunit 2 may occur through sequences carboxy-terminal to the SURP motifs. Alternative splicing results in multiple transcript variants encoding different isoforms.
Interactions
SF3A1 has been shown to interact with SF3A3 and CDC5L.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Protein%20arginine%20methyltransferase%205 | Protein arginine N-methyltransferase 5 is an enzyme that in humans is encoded by the PRMT5 gene. PRMT5 symmetrically dimethylates H2AR3, H4R3, H3R2, and H3R8 in vivo, all of which are linked to a range of transcriptional regulatory events.
PRMT5 is a highly conserved arginine methyltransferase that translocated from the cytoplasm to the nucleus at embryonic day ~E8.5, and during preimplantation development at the ~4-cell stage.
Model organisms
Model organisms have been used in the study of PRMT5 function. A conditional knockout mouse line, called Prmt5tm2a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty five tests were carried out on mutant mice and two significant abnormalities were observed. No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice but no further abnormalities were observed.
A conditional allele of Prmt5 in the mouse limb shows that it is essential for maintaining a progenitor population, as conditional mutants have limb defects
Interactions
Protein arginine methyltransferase 5 has been shown to interact with:
CLNS1A,
Janus kinase 2,
SNRPD3,
SUPT5H,
MEP50,
R |
https://en.wikipedia.org/wiki/SYNCRIP | Synaptotagmin-binding, cytoplasmic RNA-interacting protein (SYNCRIP), also known as heterogeneous nuclear ribonucleoprotein (hnRNP) Q or NS1-associated protein-1 (NSAP-1), is a protein that in humans is encoded by the SYNCRIP gene. As the name implies, SYNCRIP is localized predominantly in the cytoplasm. It is evolutionarily conserved across eukaryotes and participates in several cellular and disease pathways, especially in neuronal and muscular development. In humans, there are three isoforms, all of which are associated in vitro with pre-mRNAs, mRNA splicing intermediates, and mature mRNA-protein complexes, including mRNA turnover.
Structure and function
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA).
SYNCRIP is made up of an N-terminal helix bundle known as the “acidic domain” (AcD), followed by three sequential RNA recognition motifs (RRMs) separated by short linkers, and an arginine-glycine-rich domain called the “RGG box” at the C-terminus. The RRMs play a role in RNA binding, while the AcD engages in protein-protein interactions (PPIs). The RGG box is involved in both RNA binding and in PPIs. The AcD is unique to SYNCRIP and its nuclear homolog hnRNP R, and is involved in interactions with APOBEC-1. It is a self-folding, all-helical domain of five α-helices, containing a large hydrophobic cavity and a positively |
https://en.wikipedia.org/wiki/SORBS1 | CAP/Ponsin protein, also known as Sorbin and SH3 domain-containing protein 1 is a protein that in humans is encoded by the SORBS1 gene. It is part of a small family of adaptor proteins that regulate cell adhesion, growth factor signaling and cytoskeletal formation. It is mainly expressed in heart, skeletal muscle, liver, adipose tissue, and macrophages; in striated muscle tissue, it is localized to costamere structures.
Structure
CAP/Ponsin may exist as thirteen alternatively-spliced isoforms, ranging from 81 kDa to 142 kDa. It is part of an adaptor protein family, of which ArgBP2 and vinexin are also a part. These proteins contain a conserved sorbin homology (SOHO) domain and three SH3 domains, and CAP/Ponsin is expressed in heart, skeletal muscle, liver, adipose tissue, and macrophages.
Function
In muscle, CAP/Ponsin plays a role in the formation of mature costameres from focal adhesion-like contacts during assembly of the contractile apparatus, as overexpression of CAP/Ponsin disrupted normal cell-matrix contact morphology. In a mouse model of viral myocarditis due to Coxsackievirus infection, CAP/Ponsin stabilized antiviral type I interferon production and was protective against apoptosis and cytotoxicity. It has also been shown to be a major regulator of insulin-stimulated signaling and regulation of glucose uptake, by potentiating insulin-induced phosphorylation and recruitment of CBL to a lipid raft signaling complex involving flotillin. A role for it in macrophage |
https://en.wikipedia.org/wiki/SUB1 | Activated RNA polymerase II transcriptional coactivator p15 also known as positive cofactor 4 (PC4) or SUB1 homolog is a protein that in humans is encoded by the SUB1 gene. The human SUB1 gene is named after an orthologous gene in yeast.
SUB1 is induced by oxidative stress, and is involved in coordinating cellular responses to DNA strand breaks that arise after oxidative stress. Yeast SUB1 has structural and functional similarities to human alpha-synuclein, a protein that has an important role in Parkinson’s disease. Like SUB1, alpha-synuclein functions in regulating DNA repair including repair of DNA double-strand breaks.
Interactions
SUB1 has been shown to interact with CSTF2.
References
Further reading
External links |
https://en.wikipedia.org/wiki/PPP1R1B | Protein phosphatase 1 regulatory subunit 1B (PPP1R1B), also known as dopamine- and cAMP-regulated neuronal phosphoprotein (DARPP-32), is a protein that in humans is encoded by the PPP1R1B gene.
Function
Midbrain dopaminergic neurons play a critical role in multiple brain functions, and abnormal signaling through dopaminergic pathways has been implicated in several major neurologic and psychiatric disorders. One well studied target for the actions of dopamine is DARPP32. In the densely dopamine- and glutamate-innervated rat caudate-putamen, DARPP32 is expressed in medium-sized spiny neurons that also express dopamine D1 receptors. The function of DARPP32 seems to be regulated by receptor stimulation. Both dopaminergic and glutamatergic (NMDA) receptor stimulation regulate the extent of DARPP32 phosphorylation, but in opposite directions. Dopamine D1 receptor stimulation enhances cAMP formation, resulting in the phosphorylation of DARPP32; (this is disputed by more recent research that claims cAMP signaling induces dephosphorylation of DARPP32) phosphorylated DARPP32 is a potent protein phosphatase-1 (PPP1CA) inhibitor. NMDA receptor stimulation elevates intracellular calcium, which leads to activation of calcineurin and dephosphorylation of phospho-DARPP32, thereby reducing the phosphatase-1 inhibitory activity of DARPP32. DARPP-32 is critical for dopamine dependent striatal synaptic plasticity, possibly by serving as a dopamine-dependent gating mechanism for calcium/CaMKII |
https://en.wikipedia.org/wiki/Annexin%20A4 | Annexin A4 is a protein that in humans is encoded by the ANXA4 gene.
Function
Annexin IV (ANX4) belongs to the annexin family of calcium-dependent phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have been implicated in membrane-related events along exocytotic and endocytotic pathways. ANX4 has 45 to 59% identity with other members of its family and shares a similar size and exon-intron organization. Isolated from human placenta, ANX4 encodes a protein that has possible interactions with ATP, and has in vitro anticoagulant activity and also inhibits phospholipase A2 activity. ANX4 is almost exclusively expressed in epithelial cells.
References
External links
Further reading |
https://en.wikipedia.org/wiki/RCAN1 | Down syndrome critical region gene 1, also known as DSCR1, is a protein that in humans is encoded by the RCAN1 gene.
Gene location and organization
DSCR1 in human is located at the centromeric border of the DSCR and encodes an inhibitor of calcineurin/ NFAT (nuclear factor activated T cells) signalling.
DSCR1 genomic sequence of total 45 kb contain 7 exons and 6 introns , different cDNA analysis yield first four exons are alternative and code for two isoforms of 197 amino acids, and one isoform code for 171 amino acids which differ in their N terminal . While the rest of the 168 residues are common. There is also alternative promoter region with about 900 bp between exon 3 and 4 suggesting that the fourth isoform might be penetrated from another promoter.
Function
The protein encoded by this gene interacts with calcineurin A and inhibits calcineurin-dependent signaling pathways of genetic transcription, possibly affecting central nervous system development. Three transcript variants encoding three different isoforms have been found for this gene. In endothelial cells, VEGF stimulates RCAN1.4 expression which regulates gene expression, cell migration and tubular morphogenesis.
Structure
DSCR1 Consist of putative functional motifs and calcineurin binding domain. DSCR1 contains two proline-rich SH3 binding domain, usually named proline-rich domain (PRD), which defines the protein family. SH3 domains or PRD are very important to allow the binding of the protein to endo |
https://en.wikipedia.org/wiki/EEF1B2 | Elongation factor 1-beta is a protein that in humans is encoded by the EEF1B2 gene.
Function
This gene encodes a translation elongation factor. The protein is a guanine nucleotide exchange factor involved in the transfer of aminoacylated tRNAs to the ribosome. Alternative splicing results in three transcript variants which differ only in the 5' UTR.
Interactions
EEF1B2 has been shown to interact with EEF1G and HARS.
References
Further reading |
https://en.wikipedia.org/wiki/MARK2 | Serine/threonine-protein kinase MARK2 is an enzyme that in humans is encoded by the MARK2 gene.
Function
EMK (ELKL Motif Kinase) is a small family of ser/thr protein kinases involved in the control of cell polarity, microtubule stability and cancer. Several cDNA clones have been isolated that encoded two isoforms of the human ser/thr protein kinase EMK1. These isoforms were characterized by the presence of a 162-bp alternative exon that gave rise to two forms, one containing the exon and the other one lacking it. Both forms were found to be coexpressed in a number of selected cell lines and tissue samples. The human EMK1 was shown to be encoded by a single mRNA ubiquitously expressed.
Interactions
MARK2 has been shown to interact with AKT1.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/ERCC4 | ERCC4 is a protein designated as DNA repair endonuclease XPF that in humans is encoded by the ERCC4 gene. Together with ERCC1, ERCC4 forms the ERCC1-XPF enzyme complex that participates in DNA repair and DNA recombination.
The nuclease enzyme ERCC1-XPF cuts specific structures of DNA. Many aspects of these two gene products are described together here because they are partners during DNA repair. The ERCC1-XPF nuclease is an essential activity in the pathway of DNA nucleotide excision repair (NER). The ERCC1-XPF nuclease also functions in pathways to repair double-strand breaks in DNA, and in the repair of "crosslink" damage that harmfully links the two DNA strands.
Cells with disabling mutations in ERCC4 are more sensitive than normal to particular DNA damaging agents, including ultraviolet radiation and to chemicals that cause crosslinking between DNA strands. Genetically engineered mice with disabling mutations in ERCC4 also have defects in DNA repair, accompanied by metabolic stress-induced changes in physiology that result in premature aging. Complete deletion of ERCC4 is incompatible with viability of mice, and no human individuals have been found with complete (homozygous) deletion of ERCC4. Rare individuals in the human population harbor inherited mutations that impair the function of ERCC4. When the normal genes are absent, these mutations can lead to human syndromes, including xeroderma pigmentosum, Cockayne syndrome and Fanconi anemia.
ERCC1 and ERCC4 are the h |
https://en.wikipedia.org/wiki/Fibroblast%20activation%20protein%2C%20alpha | Fibroblast activation protein alpha (FAP-alpha) also known as prolyl endopeptidase FAP is an enzyme that in humans is encoded by the FAP gene.
Prolyl endopeptidase FAP is a 170 kDa membrane-bound gelatinase. It was independently identified as a surface glycoprotein recognized by the F19 monoclonal antibody in activated fibroblasts and a Surface Expressed Protease (seprase) in invasive melanoma cells.
Structure and enzymatic activity
FAP is a 760 amino acid long type II transmembrane glycoprotein. It contains a very short cytoplasmic N terminal part (6 amino acids), a transmembrane region (amino acids 7–26), and a large extracellular part with an alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
A soluble form of FAP, which lacks the intracellular and transmembrane part, is present in blood plasma. FAP is a non-classical serine protease, which belongs to the S9B prolyl oligopeptidase subfamily. Other members of the S9B subfamily are DPPIV, DPP8 and DPP9. FAP is most closely related to DPPIV (approximately 50% of their amino acids are identical). The active site of FAP is localized in the extracellular part of the protein and contains a catalytic triad composed of Ser624 Asp702 His734 in humans and mice. FAP is catalytically active as a 170kD homodimer and has a dipeptidase and an endopeptidase activity.
Several bioactive peptides and structural proteins were reported to be cleaved by FAP, such as neuropeptide Y (NPY), Peptide YY, Substance P (SP), a |
https://en.wikipedia.org/wiki/FGF10 | Fibroblast growth factor 10 is a protein that in humans is encoded by the FGF10 gene.
Function
The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. Fibroblast growth factor 10 is a paracrine signaling molecule seen first in the limb bud and organogenesis development. FGF10 starts the developing of limbs and its involved in the branching of morphogenesis in multiple organs such as the lungs, skin, ear and salivary glands. During the limb development Tbx4/Tbx5 stimulate the production of FGF10 in the lateral plate mesoderm where it will create an epithelial-mesenchymal FGF signal with FGF8. This positive feedback loop will increase the amount of mesenchyme resulting in a bulge. Afterwards, FGF10 will induce the formation of apical ectodermal ridge (AER) where the foot and hands will be formed. Lung development uses the same epithelial-mesenchymal signaling from FGF10 in the foregut mesenchyme with FGFR2 in the foregut epithelium. FGF10 signaling is required for epithelial branching. Therefore, all branching morphogen organs such as the lungs, skin, ear and salivary glands required the constant expression of FGF10. This protein exhibits mitogenic activity for keratinizing epidermal cells, but essentially no act |
https://en.wikipedia.org/wiki/C-fos-induced%20growth%20factor | C-fos-induced growth factor (FIGF) (or vascular endothelial growth factor D, VEGF-D) is a vascular endothelial growth factor that in humans is encoded by the FIGF gene.
Function
The protein encoded by this gene is a member of the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family and is active in angiogenesis, lymphangiogenesis, and endothelial cell growth. This secreted protein undergoes a complex proteolytic maturation, generating multiple processed forms that bind and activate VEGFR-2 and VEGFR-3 receptors. The structure and function of this protein is similar to those of vascular endothelial growth factor C.
Tumor metastasis to lymph nodes
Lymph node metastasis is very often associated with several types of human malignancies. Cancer cells’ journey to lymph node takes place largely through lymphatic tunnel located in and around of primary tumor. VEGF-D's interactions with VEGFR-3 predominantly expressed in lymphatic vessels plays a key role in restructuring lymphatic channel and, hence, able to alter its functions related to fluid and cell transport along the conduits. VEGF-D has been established to be over-expressed in both tumor tissues and patients’ serum samples in several types of human cancer. In addition, VEGF-D expression has been implicated with increased incidence of regional lymph node metastasis. In experimental mice study, genetically modified tumor cell that was forced to produce VEGF-D protein have been established to |
https://en.wikipedia.org/wiki/Rolls-Royce%20Merlin%20alternative%20uses | The Rolls-Royce Merlin, although designed as an aero engine, was used in other applications both on land and at sea. A derivative called the Meteor was developed for use in tanks.
Automotive
Michael Wilcock of Sussex, England, built the Swandean Spitfire Special, using a Merlin XXV engine acquired from a scrap yard for one hundred and forty pounds. The engine was installed in a home-brewed chassis confected from two Daimler Dingo scout car chassis. The car was run in the Brighton Speed Trials in 1953, and was sold to James Duffy of St. Louis, Missouri, in 1956. As of 2005, the vehicle is still in St. Louis, where it is undergoing restoration.
The Beast
In the 1960s, engineer Paul Jameson put a Rolls-Royce Meteor engine into a chassis he built himself. He did not get around to building a body, and sold the car to Epsom-based automatic transmission specialist John Dodd, who had supplied the automatic gearbox. Fibre Glass Repairs in Bromley, Kent, fitted a fibreglass body, based around a modified Ford Capri 'funny car' bodyshell, and the finished car, registered in the UK in 1972, was named The Beast. The Beast was extremely popular at car shows all over Europe, featuring in numerous custom car publications in the 1970s and 1980s. It was once listed in the Guinness Book of Records as the world's most powerful road car.
At some point in the late 1970s or early 1980s, the first iteration of the Beast caught fire on the way back from a car show in Stockholm (a trip during wh |
https://en.wikipedia.org/wiki/GNB2 | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2 is a protein that in humans is encoded by the GNB2 gene.
Heterotrimeric guanine nucleotide-binding proteins (G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes.
This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. This gene contains a trinucleotide (CCG) repeat length polymorphism in its 5' UTR.
References
Further reading |
https://en.wikipedia.org/wiki/GYPB | Glycophorin B (MNS blood group) (gene designation GYPB) also known as sialoglycoprotein delta and SS-active sialoglycoprotein is a protein which in humans is encoded by the GYPB gene. GYPB has also recently been designated CD235b (cluster of differentiation 235b).
Function
Glycophorin A (GYPA) and B (GYPB; this protein) are major sialoglycoproteins of the human erythrocyte membrane which bear the antigenic determinants for the MN and Ss blood groups respectively. In addition to the M or N and S or s antigens, that commonly occur in all populations, about 40 related variant phenotypes have been identified. These variants include the Miltenberger (Mi) complex and several isoforms of Stones (Sta); also Dantu, Sat, Henshaw (He or MNS6), Mg and deletion variants Ena, S-s-U- and Mk. Most of these are the result of gene recombinations between GYPA and GYPB.
Genomics
The gene is located on the long arm of chromosome 4 (4q28-q31) and has 5 exons. It was first sequenced in 1987 the peptide sequence of 72 amino acids having been determined earlier that year.
The gene has 97% sequence homology with the glycophorin A gene from the 5' UTR approximately 1 kilobase upstream from the exon encoding the transmembrane regions to the portion of the coding sequence encoding the first 45 amino acids. There is a signal sequence of 19 amino acid residues. The leader peptide differs by one amino acid and the next 26 amino acids are identical. Amino acids 27-55 of glycophorin A are absent from g |
https://en.wikipedia.org/wiki/HMGB2 | High-mobility group protein B2 also known as high-mobility group protein 2 (HMG-2) is a protein that in humans is encoded by the HMGB2 gene.
Function
This gene encodes a member of the non-histone chromosomal high-mobility group protein family. The proteins of this family are chromatin-associated and ubiquitously distributed in the nucleus of higher eukaryotic cells. In vitro studies have demonstrated that this protein is able to efficiently bend DNA and form DNA circles. These studies suggest a role in facilitating cooperative interactions between cis-acting proteins by promoting DNA flexibility. This protein was also reported to be involved in the final ligation step in DNA end-joining processes of DNA double-strand breaks repair and V(D)J recombination.
References
Further reading
Loss of HMGB2 (High-mobility group protein box 2) during senescence blunts SASP (senescence-associated secretory phenotype) gene expression by allowing for spreading of repressive heterochromatin into SASP gene loci. This correlates with incorporation of SASP gene loci into SAHF (senescence-associated heterochromatin foci), which in turn represses SASP gene expression
External links
Transcription factors |
https://en.wikipedia.org/wiki/HNRPF | Heterogeneous nuclear ribonucleoprotein F is a protein that in humans is encoded by the HNRNPF gene.
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins that complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and regulate alternative splicing, polyadenylation, and other aspects of mRNA metabolism and transport.
While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has three repeats of quasi-RRM domains that bind to RNAs which have guanosine-rich sequences. This protein is very similar to the family member hnRNPH. Multiple alternatively spliced variants, encoding the same protein, have been identified.
References
Further reading |
https://en.wikipedia.org/wiki/HOXD10 | Homeobox D10, also known as HOXD10, is a protein which in humans is encoded by the HOXD10 gene.
Function
This gene is a member of the Abd-B homeobox family and encodes a protein with a homeobox DNA-binding domain. It is included in a cluster of homeobox D genes located on chromosome 2. The encoded nuclear protein functions as a sequence-specific transcription factor that is expressed in the developing limb buds and is involved in differentiation and limb development.
Clinical significance
Mutations in this gene have been associated with Wilms' tumor and congenital vertical talus (also known as "rocker-bottom foot" deformity or congenital convex pes valgus) and/or a foot deformity resembling that seen in Charcot-Marie-Tooth disease.
Regulation
The HOXD10 gene is repressed by the microRNAs miR-10a and miR-10b.
See also
Homeobox
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/IRF4 | Interferon regulatory factor 4 (IRF4) also known as MUM1 is a protein that in humans is encoded by the IRF4 gene,. IRF4 functions as a key regulatory transcription factor in the development of human immune cells. The expression of IRF4 is essential for the differentiation of T lymphocytes and B lymphocytes as well as certain myeloid cells. Dysregulation of the IRF4 gene can result in IRF4 functioning either as an oncogene or a tumor-suppressor, depending on the context of the modification.
The MUM1 symbol is also the current HGNC official symbol for melanoma associated antigen (mutated) 1 (HGNC:29641).
Immune cell development
IRF4 is a transcription factor belonging to the Interferon Regulatory Factor (IRF) family of transcription factors. In contrast to some other IRF family members, IRF4 expression is not initiated by interferons; rather, IRF4 expression is promoted by a variety of bioactive stimuli, including antigen receptor engagement, lipopolysaccharide (LPS), IL-4, and CD40. IRF4 can function either as an activating or an inhibitory transcription factor depending on its transcription cofactors. IRF4 frequently cooperates with the cofactors B-cell lymphoma 6 protein (BCL6) and nuclear factor of activated T-cells (NFATs). IRF4 expression is limited to cells of the immune system, in particular T cells, B cells, macrophages and dendritic cells.
T cell differentiation
IRF4 plays an important role in the regulation of T cell differentiation. In particular, IRF4 ensures |
https://en.wikipedia.org/wiki/Jean-Fran%C3%A7ois%20Le%20Gall | Jean-François Le Gall (born 15 November 1959) is a French mathematician working in areas of probability theory such as Brownian motion, Lévy processes, superprocesses and their connections with partial differential equations, the Brownian snake, random trees, branching processes, stochastic coalescence and random planar maps. He received his Ph.D. in 1982 from Pierre and Marie Curie University (Paris VI) under the supervision of Marc Yor. He is currently professor at the University of Paris-Sud in Orsay and is a senior member of the Institut universitaire de France. He was elected to French academy of sciences, December 2013.
He was awarded the Rollo Davidson Prize in 1986, the Loève Prize in 1997, and the Fermat Prize in 2005. He was the thesis advisor of at least 11 students including Wendelin Werner. For 2019 he received the Wolf Prize in Mathematics. and for 2021 he was awarded the BBVA Foundation Frontiers of Knowledge Award in Basic Sciences.
Books
Le Gall, Jean-François, Spatial branching processes, random snakes and partial differential equations. Lectures in Mathematics ETH Zürich. Birkhäuser Verlag, Basel (1999). 163 pp.
Le Gall, Jean-François, Brownian Motion, Martingales, and Stochastic Calculus. Graduate Texts in Mathematics. Springer International Publishing Switzerland (2016).
References
External links
professional page
20th-century French mathematicians
21st-century French mathematicians
Academic staff of Paris-Sud University
Probability theorists
É |
https://en.wikipedia.org/wiki/LRP6 | Low-density lipoprotein receptor-related protein 6 is a protein that in humans is encoded by the LRP6 gene. LRP6 is a key component of the LRP5/LRP6/Frizzled co-receptor group that is involved in canonical Wnt pathway.
Structure
LRP6 is a transmembrane low-density lipoprotein receptor that shares a similar structure with LRP5. In each protein, about 85% of its 1600-amino-acid length is extracellular. Each has four β-propeller motifs at the amino terminal end that alternate with four epidermal growth factor (EGF)-like repeats. Most extracellular ligands bind to LRP5 and LRP6 at the β-propellers. Each protein has a single-pass, 22-amino-acid segment that crosses the cell membrane and a 207-amino-acid segment that is internal to the cell.
Function
LRP6 acts as a co-receptor with LRP5 and the Frizzled protein family members for transducing signals by Wnt proteins through the canonical Wnt pathway.
Interactions
Canonical WNT signals are transduced through Frizzled receptor and LRP5/LRP6 coreceptor to downregulate GSK3beta (GSK3B) activity not depending on Ser-9 phosphorylation. Reduction of canonical Wnt signals upon depletion of LRP5 and LRP6 results in p120-catenin degradation.
LRP6 is regulated by extracellular proteins in the Dickkopf (Dkk) family (like DKK1), sclerostin, R-spondins and members of the cysteine-knot-type protein family.
Clinical significance
Loss-of-function mutations or LRP6 in humans lead to increased plasma LDL and triglycerides, hypertension, diabetes |
https://en.wikipedia.org/wiki/MCM5 | DNA replication licensing factor MCM5 is a protein that in humans is encoded by the MCM5 gene.
Function
The protein encoded by this gene is structurally very similar to the CDC46 protein from S. cerevisiae, a protein involved in the initiation of DNA replication. The encoded protein is a member of the MCM family of chromatin-binding proteins and can interact with at least two other members of this family. The encoded protein is upregulated in the transition from the G0 to G1/S phase of the cell cycle and may actively participate in cell cycle regulation.
See also
Mini Chromosome Maintenance
Interactions
MCM5 has been shown to interact with:
Cell division cycle 7-related protein kinase,
MCM2,
MCM3,
MCM7,
ORC2L,
ORC6L, and
STAT1.
References
Further reading |
https://en.wikipedia.org/wiki/Lens%20fiber%20major%20intrinsic%20protein | Lens fiber major intrinsic protein also known as aquaporin-0 is a protein that in humans is encoded by the MIP gene.
Function
Major intrinsic protein is a member of the water-transporting aquaporins as well as the original member of the MIP family of channel proteins. The function of the fiber cell membrane protein encoded by this gene is undetermined, yet this protein is speculated to play a role in intracellular communication. The MIP protein is expressed in the ocular lens and is required for correct lens function. This gene has been mapped among aquaporins AQP2, AQP5, and AQP6, in a potential gene cluster at 12q13.
References
Further reading |
https://en.wikipedia.org/wiki/MXI1 | MAX-interacting protein 1 is a protein that in humans is encoded by the MXI1 gene.
Function
Expression of the c-myc gene, which produces an oncogenic transcription factor, is tightly regulated in normal cells but is frequently deregulated in human cancers. The protein encoded by this gene is a transcriptional repressor thought to negatively regulate MYC function, and is therefore a potential tumor suppressor. This protein inhibits the transcriptional activity of MYC by competing for MAX, another basic helix-loop-helix protein that binds to MYC and is required for its function. Defects in this gene are frequently found in patients with prostate tumors. Three alternatively spliced transcripts encoding different isoforms have been described. Additional alternatively spliced transcripts may exist but the products of these transcripts have not been verified experimentally.
Interactions
MXI1 has been shown to interact with SMC3 and MAX.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/NCOA6 | Nuclear receptor coactivator 6 is a protein that in humans is encoded by the NCOA6 gene.
Function
The protein encoded by this gene is a transcriptional coactivator that can interact with nuclear hormone receptors to enhance their transcriptional activator functions. The encoded protein has been shown to be involved in the hormone-dependent coactivation of several receptors, including prostanoid, retinoid, vitamin D3, thyroid hormone, and steroid receptors. The encoded protein may also act as a general coactivator since it has been shown to interact with some basal transcription factors, histone acetyltransferases, and methyltransferases.
Interactions
NCOA6 has been shown to interact with:
ASCL2 and
Activating transcription factor 2,
Androgen receptor,
CREB-binding protein,
DNA-PKcs,
E2F1,
EP300,
Estrogen receptor alpha,
Estrogen receptor beta,
HBXIP,
HIST2H3C,
HSF1,
Ku70,
Ku80,
Liver X receptor beta,
MLL3,
RBBP5,
Retinoblastoma protein,
Retinoic acid receptor alpha,
Retinoid X receptor alpha,
Src,
TGS1,
TUBA4A,
TUBB,
Thyroid hormone receptor alpha, and
Thyroid hormone receptor beta.
See also
Transcription coregulator
References
Further reading
External links
Gene expression
Transcription coregulators
Human proteins |
https://en.wikipedia.org/wiki/MAP3K7IP2 | Mitogen-activated protein kinase kinase kinase 7-interacting protein 2 is an enzyme that in humans is encoded by the MAP3K7IP2 gene.
The protein encoded by this gene is an activator of MAP3K7/TAK1, which is required for the IL-1 induced activation of nuclear factor kappaB and MAPK8/JNK. This protein forms a kinase complex with TRAF6, MAP3K7 and TAB1, thus serves as an adaptor linking MAP3K7 and TRAF6. This protein, TAB1, and MAP3K7 also participate in the signal transduction induced by TNFSF11/RANKL through the activation of the receptor activator of NF-kappB (TNFRSF11A/RANK), which may regulate the development and function of osteoclasts. Mutations in MAP3K7IP2 have been associated with human congenital heart defects.
Interactions
MAP3K7IP2 has been shown to interact with:
HDAC3,
TAB1,
MAP3K7IP3,
MAP3K7,
NFKB1,
NUMBL,
Nuclear receptor co-repressor 1,
TRAF2, and
TRAF6.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Transmembrane%20activator%20and%20CAML%20interactor | Transmembrane activator and CAML interactor (TACI), also known as tumor necrosis factor receptor superfamily member 13B (TNFRSF13B) is a protein that in humans is encoded by the TNFRSF13B gene.
TNFRSF13B is a transmembrane protein of the TNF receptor superfamily found predominantly on the surface of B cells, which are an important part of the immune system. TACI recognizes three ligands: APRIL, BAFF and CAML.
Function
TACI is a lymphocyte-specific member of the tumor necrosis factor (TNF) receptor superfamily. It was originally discovered because of its ability to interact with calcium-modulator and cyclophilin ligand (CAML). TACI was later found to play a crucial role in humoral immunity by interacting with two members of the TNF family: BAFF and APRIL. These proteins signal through TACI inducing activation of several transcription factors including NFAT, AP-1, and NF-kappa-B which then modulate cellular activities. Defects in the function of TACI can lead to immune system diseases and has shown to cause fatal autoimmunity in mice.
TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
Clinical significance
TACI mutations are associated with immunodeficiency in humans, as a significant proportion of CVID patients have TACI mutations. People with this condition produce abnormally low amounts of antibodies, which are needed for protection against infections.
In humans, the gene encoding this protein is located within th |
https://en.wikipedia.org/wiki/RBMX | Heterogeneous nuclear ribonucleoprotein G is a protein that in humans is encoded by the RBMX gene.
Function
This gene belongs to the RBMY gene family which includes candidate Y chromosome spermatogenesis genes. This gene, an active X chromosome homolog of the Y chromosome RBMY gene, is widely expressed whereas the RBMY gene evolved a male-specific function in spermatogenesis. Pseudogenes of this gene, found on chromosomes 1, 4, 9, 11, and 6, were likely derived by retrotransposition from the original gene. Alternatively spliced transcript variants encoding different isoforms have been identified but their biological nature has not been determined.
Interactions
RBMX has been shown to interact with SFRS10 and CDC5L.
Model organisms
Model organisms have been used in the study of RBMX function. A conditional knockout mouse line called Rbmxtm2b(KOMP)Wtsi 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 |
https://en.wikipedia.org/wiki/GIT1 | ARF GTPase-activating protein GIT1 is an enzyme that in humans is encoded by the GIT1 gene.
GIT1 contains an ARFGAP domain, Anykrin repeats, and a GRK-interacting domain. The Arf-GAP domain, which enables it to act as a GTPase activating protein (GAP) for the Arf family of GTPases, has been shown to be involved in phosphorylation and inhibition of the ADRB2. If synaptic localization of GIT1 is disturbed, then this is known to affect dendritic spine morphology and formation---this is thought to occur through the Rac1/PAK1/LIMK/CFL1 pathway.
Interactions
GIT1 has been shown to interact with:
ARHGEF7,
Beta adrenergic receptor kinase,
GIT2,
PCLO,
PLCG1,
PPFIA4
PTK2, and
liprin-alpha-1.
References
Further reading
External links
GIT1 Info with links in the Cell Migration Gateway |
https://en.wikipedia.org/wiki/KCNIP2 | Kv channel-interacting protein 2 also known as KChIP2 is a protein that in humans is encoded by the KCNIP2 gene.
Function
This gene encodes a member of the family of voltage-gated potassium (Kv) channel-interacting proteins (KCNIPs, also frequently called "KChIP"), which belong to the recoverin branch of the EF-hand superfamily. Members of the KCNIP family are small calcium binding proteins. They all have EF-hand-like domains, and differ from each other in the N-terminus. They are integral subunit components of native Kv4 channel complexes. They may regulate A-type currents, and hence neuronal excitability, in response to changes in intracellular calcium. Alternative splicing results in multiple transcript variant encoding different isoforms.
See also
Voltage-gated potassium channel
References
Further reading
External links
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/ATP5B | ATP synthase F1 subunit beta, mitochondrial is an enzyme that in humans is encoded by the ATP5F1B gene.
Function
This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the beta subunit of the catalytic core.
References
External links
Further reading |
https://en.wikipedia.org/wiki/ATP6V1B1 | V-type proton ATPase subunit B, kidney isoform is an enzyme that in humans is encoded by the ATP6V1B1 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 and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c' ', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness.
References
External links
Further reading |
https://en.wikipedia.org/wiki/MYH10 | Myosin-10 also known as myosin heavy chain 10 or non-muscle myosin IIB (NM-IIB) is a protein that in humans is encoded by the MYH10 gene. Non-muscle myosins are expressed in a wide variety of tissues, but NM-IIB is the only non-muscle myosin II isoform expressed in cardiac muscle, where it localizes to adherens junctions within intercalated discs. NM-IIB is essential for normal development of cardiac muscle and for integrity of intercalated discs. Mutations in MYH10 have been identified in patients with left atrial enlargement.
Structure
NM-IIB is 228.9 kDa protein composed of 1976 amino acids. NM-IIB has an N-terminal globular head that harbors the catalytically active, magnesium(Mg)-ATPase. The C-terminal rod domain is an alpha helical coiled-coil that can multimerize with other myosin molecules to form a filament. Bound to the neck region of NM-IIB are two light chains; first, MLC17 stabilizes the molecule, while the second light chain, MLC20, modulates contraction. The exception to this rule is the alternatively spliced NM-IIB2 isoform, which has a 21 amino acid inserted into loop 2, near the actin-binding domain; actomyosin MgATPase activity of this isoform is not enhanced by phosphorylation of the regulatory light chain MLC20.
NM-IIB is part of the larger myosin II subfamily of proteins, which also includes skeletal muscle, cardiac muscle and smooth muscle myosins. NM-IIB, and non-muscle myosins in general, are widely expressed in every tissue in humans.
Function
|
https://en.wikipedia.org/wiki/Poly%28A%29-specific%20ribonuclease | Poly(A)-specific ribonuclease (PARN), also known as polyadenylate-specific ribonuclease or deadenylating nuclease (DAN), is an enzyme that in humans is encoded by the PARN gene.
Function
Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. The amino acid sequence of poly(A)-specific ribonuclease shows homology to the RNase D family of 3'-exonucleases. The protein appears to be localized in both the nucleus and the cytoplasm. It is not stably associated with polysomes or ribosomal subunits. Hereditary mutations in PARN lead to the bone marrow failure disease dyskeratosis congenita which is caused by defective telomerase RNA processing and degradation in patients.
References
Further reading
EC 3.1.13 |
https://en.wikipedia.org/wiki/PDE4A | cAMP-specific 3',5'-cyclic phosphodiesterase 4A is an enzyme that in humans is encoded by the PDE4A gene.
Function
The protein encoded by this gene belongs to the cyclic nucleotide phosphodiesterase (PDE) family, and PDE4 subfamily. This PDE hydrolyzes the secondary messenger, cAMP, which is a regulator and mediator of a number of cellular responses to extracellular signals. Thus, by regulating the cellular concentration of cAMP, this protein plays a key role in many important physiological processes. Recently, it has been shown through the use of PDE4A knock out mice that PDE4A may play a role in the regulation of anxiety and emotional memory.
Clinical significance
PDE4A inhibition is a target of a number of drugs including:
rolipram (antidepressant and antiinflammatory) and cilomilast (antiinflammatory) – inhibits PDE4A isoforms 1, 2, 6, and 7
roflumilast (antiinflammatory) – inhibits PDE4A isoforms 1, 2, and 6
References
Further reading |
https://en.wikipedia.org/wiki/PFKM | 6-phosphofructokinase, muscle type is an enzyme that in humans is encoded by the PFKM gene on chromosome 12.
Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. These isozymes function as subunits of the mammalian tetramer phosphofructokinase, which catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate. Tetramer composition varies depending on tissue type. This gene encodes the muscle-type isozyme. Mutations in this gene have been associated with glycogen storage disease type VII, also known as Tarui disease. Alternatively spliced transcript variants have been described.[provided by RefSeq, Nov 2009]
Structure
Gene
This gene is found on chromosome 12. The coding region in PFKM only shares a 68% similarity with that of the liver-type PFKL.
Protein
This 85-kDa protein is one of two subunit types that comprise the seven tetrameric PFK isozymes. The muscle isozyme (PFK-1) is composed solely of PFKM.
The liver PFK (PFK-5) contains solely the second subunit type, PFKL, while the erythrocyte PFK includes five isozymes composed of different combinations of PFKM and PFKL. These subunits evolved from a common prokaryotic ancestor via gene duplication and mutation events. Generally, the N-terminal of the subunits carries out their catalytic activity while the C-terminal contains allosteric ligand binding sites. In particular, the binding site for the PFK inhibitor citrate is found in the PFKL C-terminal region.
Function
Th |
https://en.wikipedia.org/wiki/Progastricsin | Progastricsin also known as pepsinogen C or pepsinogen II is a pepsinogen precursor of the enzyme gastricsin that in humans is encoded by the PGC gene.
Function
Progastricsin is an aspartic proteinase that belongs to the peptidase family A1. The encoded protein is a digestive enzyme that is produced in the stomach and constitutes a major component of the gastric mucosa. This protein is also secreted into the serum. This protein is synthesized as an inactive zymogen that includes a highly basic prosegment. This enzyme is converted into its active mature form at low pH by sequential cleavage of the prosegment that is carried out by the enzyme itself.
Clinical significance
Polymorphisms in this gene are associated with susceptibility to gastric cancers. Serum levels of this enzyme are used as a biomarker for certain gastric diseases including Helicobacter pylori related gastritis.
See also
Pepsinogen
References
Further reading
EC 3.4.23 |
https://en.wikipedia.org/wiki/PLA2G5 | Calcium-dependent phospholipase A2 is an enzyme that in humans is encoded by the PLA2G5 gene.
This gene is a member of the secretory phospholipase A2 family. It is located in a tightly-linked cluster of secretory phospholipase A2 genes on chromosome 1. The encoded enzyme catalyzes the hydrolysis of membrane phospholipids to generate lysophospholipids and free fatty acids including arachidonic acid. It preferentially hydrolyzes linoleoyl-containing phosphatidylcholine substrates. Secretion of this enzyme is thought to induce inflammatory responses in neighboring cells. Alternatively spliced transcript variants have been found, but their full-length nature has not been determined.
References
Further reading |
https://en.wikipedia.org/wiki/PLAGL1 | Zinc finger protein PLAGL1 is a protein that in humans is encoded by the PLAGL1 gene.
Function
This gene encodes a C2H2 zinc finger protein with transactivation and DNA-binding activity. This gene has been shown to exhibit antiproliferative activities and is a tumor suppressor gene candidate. Many transcript variants encoding two different isoforms have been found for this gene.
Interactions
PLAGL1 has been shown to interact with P53.
References
Further reading |
https://en.wikipedia.org/wiki/PLCB3 | 1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3 is an enzyme that in humans is encoded by the PLCB3 gene.
The gene codes for the enzyme phospholipase C β3. The enzyme catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of many extracellular signals. This gene is activated by two G-protein alpha subunits, alpha-q and alpha-11, as well as G-beta gamma subunits.
Interactions
PLCB3 has been shown to interact with Sodium-hydrogen exchange regulatory cofactor 2.
References
Further reading
EC 3.1.4 |
https://en.wikipedia.org/wiki/PLCD1 | 1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1 is an enzyme that in humans is encoded by the PLCD1 gene.
PLCd1 is essential to maintain homeostasis of the skin.
See also
Phospholipase C
References
Further reading
External links
WikiGenes entry for PLCD1
EC 3.1.4
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/Pinin | Pinin is a protein that in humans is encoded by the PNN gene.
Interactions
Pinin has been shown to interact with Keratin 8, Keratin 18, Keratin 19, CTBP1, RNPS1, PRPF4B, SFRS4, PPIG, SRRM2 and SFRS18.
References
Further reading |
https://en.wikipedia.org/wiki/PON2 | Serum paraoxonase/arylesterase 2 is an enzyme that in humans is encoded by the PON2 gene.
This gene encodes a member of the paraoxonase gene family, which includes three known members located adjacent to each other on the long arm of chromosome 7. The encoded protein is ubiquitously expressed in human tissues, membrane-bound, and may act as a cellular antioxidant, protecting cells from oxidative stress. Hydrolytic activity against acylhomoserine lactones, important bacterial quorum-sensing mediators, suggests the encoded protein may also play a role in defense responses to pathogenic bacteria. Mutations in this gene may be associated with vascular disease and a number of quantitative phenotypes related to diabetes. Alternatively spliced transcript variants encoding different isoforms have been described.
References
Further reading |
https://en.wikipedia.org/wiki/Serglycin | Serglycin, also known as hematopoietic proteoglycan core protein or secretory granule proteoglycan core protein, is a protein that in humans is encoded by the SRGN gene. It is primarily expressed in hematopoietic cells and endothelial cells, and is the only known intracellular proteoglycan.
Function
This gene encodes a protein best known as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of many hematopoietic cells also contain a protease-resistant peptide core, which may be important for neutralizing hydrolytic enzymes. This encoded protein was found to be associated with the macromolecular complex of granzymes and perforin, and serves as a scaffold for the granzyme and perforin in granule-mediated apoptosis.
References
Further reading
Proteoglycans |
https://en.wikipedia.org/wiki/PTPRE | Receptor-type tyrosine-protein phosphatase epsilon is an enzyme that in humans is encoded by the PTPRE gene.
Function
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. Two alternatively spliced transcript variants of this gene have been reported, one of which encodes a receptor-type PTP that possesses a short extracellular domain, a single transmembrane region, and two tandem intracytoplasmic catalytic domains; Another one encodes a PTP that contains a distinct hydrophilic N-terminus, and thus represents a nonreceptor-type isoform of this PTP. Studies of the similar gene in mice suggested the regulatory roles of this PTP in RAS related signal transduction pathways, cytokines induced SATA signaling, as well as the activation of voltage-gated K+ channels.
Interactions
PTPRE has been shown to interact with KCNB1.
References
Further reading |
https://en.wikipedia.org/wiki/60S%20ribosomal%20protein%20L7a | 60S ribosomal protein L7a is a protein that in humans is encoded by the RPL7A gene.
Cytoplasmic ribosomes, organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L7AE family of ribosomal proteins. It can interact with a subclass of nuclear hormone receptors, including thyroid hormone receptor, and inhibit their ability to transactivate by preventing their binding to their DNA response elements. This gene is included in the surfeit gene cluster, a group of very tightly linked genes that do not share sequence similarity. It is co-transcribed with the U24, U36a, U36b, and U36c small nucleolar RNA genes, which are located in its second, fifth, fourth, and sixth introns, respectively. This gene rearranges with the trk proto-oncogene to form the chimeric oncogene trk-2h, which encodes an oncoprotein consisting of the N terminus of ribosomal protein L7a fused to the receptor tyrosine kinase domain of trk. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
References
Further reading
Ribosomal proteins |
https://en.wikipedia.org/wiki/40S%20ribosomal%20protein%20S3 | 40S ribosomal protein S3 is a protein that in humans is encoded by the RPS3 gene.
Function
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit, where it forms part of the domain where translation is initiated. The protein belongs to the S3P family of ribosomal proteins. Studies of the mouse and rat proteins have demonstrated that the protein has an extraribosomal role as an endonuclease involved in the repair of UV-induced DNA damage. The protein appears to be located in both the cytoplasm and nucleus but not in the nucleolus. Higher levels of expression of this gene in colon adenocarcinomas and adenomatous polyps compared to adjacent normal colonic mucosa have been observed. This gene is co-transcribed with the small nucleolar RNA genes U15A and U15B, which are located in its first and fifth introns, respectively. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
References
Further reading
Ribosomal proteins |
https://en.wikipedia.org/wiki/40S%20ribosomal%20protein%20S3a | 40S ribosomal protein S3a is a protein that in humans is encoded by the RPS3A gene.
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S3AE family of ribosomal proteins. It is located in the cytoplasm. Disruption of the gene encoding rat ribosomal protein S3a, also named v-fos transformation effector protein, in v-fos-transformed rat cells results in reversion of the transformed phenotype. Transcript variants utilizing alternative transcription start sites have been described. This gene is co-transcribed with the U73A and U73B small nucleolar RNA genes, which are located in its fourth and third introns, respectively. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
Interactions
RPS3A has been shown to interact with DNA damage-inducible transcript 3.
References
Further reading
Ribosomal proteins |
https://en.wikipedia.org/wiki/RRAS | Ras-related protein R-Ras is a protein that in humans is encoded by the RRAS gene.
Interactions
RRAS has been shown to interact with:
ARAF,
Bcl-2,
NCK1,
RALGDS, and
RASSF5.
References
Further reading |
https://en.wikipedia.org/wiki/S100A12 | S100 calcium-binding protein A12 (S100A12) is a protein that in humans is encoded by the S100A12 gene. Human S100A12, also known as calgranulin C, was first described in 1995.
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs.
Function
Generally, S100A12 has a significant anti-infectious and antibacterial role that is related to its ability to uptake ions. For example, it inhibits the spread and virulence of H. pylori.
Tissue distribution
Neutrophils and monocytes / macrophages are important source of S100A12 in the cell although some epithelial cells and dendritic cells are capable of its secretion. Some tissues are rich in these cells, and so in this protein. These include the spleen or lungs. It occurs intracellularly but is also produced into the extracellular environment where it occurs as a homodimer or hexamer.
Clinical significance
Its presence is associated with cardiovascular and kidney diseases. Like other S100 proteins, S100A12 signals through the RAGE receptor and TLR. In general, this signalling leads to cytokine production, chemotaxis and increased oxidative stress. In endothelial cells, this signaling leads to activation of NFκB, under which the production of adhesion molecules such as ICAMs, VCAM or selectins is increased. This protein is proposed to be involved in specific calcium-dependent signal transduction pathways and its regulatory effect on cytoskeletal components may modu |
https://en.wikipedia.org/wiki/ANGPTL4 | Angiopoietin-like 4 is a protein that in humans is encoded by the ANGPTL4 gene. Alternatively spliced transcript variants encoded with different isoforms have been described. This gene was previously referred to as ANGPTL2, HFARP, PGAR, or FIAF but has been renamed ANGPTL4.
This gene is induced under hypoxic (low oxygen) condition in various cell types and is the target of peroxisome proliferator-activated receptors. The encoded protein is a serum hormone directly involved in regulating lipid metabolism.
ANGPTL4 plays an important role in numerous cancers and is implicated in the metastatic process by modulating vascular permeability, cancer cell motility and invasiveness.
Name
The former name, FIAF, stands for Fasting-Induced Adipose Factor.
Structure
This gene is a member of the angiopoietin-like gene family and encodes a glycosylated, secreted protein with a coiled-coil N-terminal domain and a fibrinogen-like C-terminal domain.
Expression
In mice, the highest mRNA expression levels of ANGPTL4 are found in white and brown adipose tissue, followed by liver, kidney, muscle and intestinal tissues. Human ANGPTL4 is most highly expressed in the liver as a hepatokine.
Function
This gene is induced under hypoxic (low oxygen) condition in various cell types and is the target of peroxisome proliferator-activated receptors. The encoded protein is a serum hormone directly involved in regulating lipid metabolism. The native full length ANGPTL4 can form higher order struct |
https://en.wikipedia.org/wiki/GNG2 | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 is a protein that in humans is encoded by the GNG2 gene.
Heterotrimeric G proteins play vital roles in cellular responses to external signals. The specificity of a G protein-receptor interaction is primarily mediated by the gamma subunit.[supplied by OMIM]
Interactive pathway map
References
Further reading |
https://en.wikipedia.org/wiki/UGT1A10 | UDP-glucuronosyltransferase 1-10 is an enzyme that in humans is encoded by the UGT1A10 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. The enzyme encoded by this gene has glucuronidase activity on mycophenolic acid, coumarins, and quinolines.
Interactive pathway map
References
Further reading |
https://en.wikipedia.org/wiki/CHFR | E3 ubiquitin-protein ligase CHFR is an enzyme that in humans is encoded by the CHFR gene.
CHFR is recruited to sites of DNA damage and participates in the DNA damage response. CHFR has an important role in the survival of male premeiotic germ cells. About 30% of male CHFR knockout mice are infertile. In these knockout mice spermatogenesis onset is delayed and apoptosis in premeiotic germ cells is significantly increased. When these mice are 3 months old there is a complete loss of germ cells in their testes.
References
External links
Further reading |
https://en.wikipedia.org/wiki/ALS2 | Alsin is a protein that in humans is encoded by the ALS2 gene. ALS2 orthologs have been identified in all mammals for which complete genome data are available.
See also
Juvenile primary lateral sclerosis
Amyotrophic lateral sclerosis
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on ALS2-Related Disorders
OMIM entries on ALS2-Related Disorders
Genetics Home Reference- US National Library of Medicine® |
https://en.wikipedia.org/wiki/BMX%20%28gene%29 | Cytoplasmic tyrosine-protein kinase BMX is an enzyme that in humans is encoded by the BMX gene.
Function
Tyrosine kinases are either receptor molecules, which contain transmembrane and extracellular domains, or nonreceptor proteins, which are located intracellularly. One family of nonreceptor TKs includes the genes TEC, TXK, ITK, and BTK. All of these proteins are homologs of the Drosophila Src28 TK and contain an SH3 and SH2 domain upstream of the TK domain.
Interactions
BMX has been shown to interact with:
PAK1,
PTK2,
PTPN21 and
RUFY1.
References
Further reading
External links
Tyrosine kinases |
https://en.wikipedia.org/wiki/CCNC%20%28gene%29 | Cyclin-C is a protein that in humans is encoded by the CCNC gene.
The protein encoded by this gene is a member of the cyclin family of proteins. The encoded protein interacts with cyclin-dependent kinase 8 and induces the phosphorylation of the carboxy-terminal domain of the large subunit of RNA polymerase II. The level of mRNAs for this gene peaks in the G1 phase of the cell cycle. Two transcript variants encoding different isoforms have been found for this gene.
Interactions
CCNC (gene) has been shown to interact with Estrogen receptor alpha and Cyclin-dependent kinase 8.
References
External links
Further reading |
https://en.wikipedia.org/wiki/Cyclin-dependent%20kinase%208 | Cell division protein kinase 8 is an enzyme that in humans is encoded by the CDK8 gene.
Function
The protein encoded by this gene is a member of the cyclin-dependent protein kinase (CDK) family. CDK8 and cyclin C associate with the mediator complex and regulate transcription by several mechanisms. CDK8 binds to and/or phosphorylates several transcription factors, which can have an activating or inhibitory effect on transcription factor function. CDK8 phosphorylates the Notch intracellular domain, SREBP, and STAT1 S727. CDK8 also inhibits transcriptional activation by influencing turnover of subunits in the mediator complex tail module. In addition, CDK8 influences binding of RNA polymerase II to the mediator complex.
Clinical significance
CDK8 is a colorectal cancer oncogene: the CDK8 gene is amplified in human colorectal tumors, activating β-catenin-mediated transcription that drives colon tumorigenesis. However, CDK8 may not be oncogenic in all cell types, and indeed may act as a tumor suppressor in the notch and EGFR signaling pathways. Specifically, CDK8 promotes turnover of the notch intracellular domain, and inhibits EGFR signaling-driven cell fates in C. elegans. Thus, CDK8 may be an oncogene in cancers driven by Wnt/β-catenin signaling, but could instead be a tumor suppressor gene in cancers driven by notch or EGFR signaling. In addition, CDK8 promotes transcriptional activation mediated by the tumor suppressor protein p53, indicating that it may have an importa |
https://en.wikipedia.org/wiki/SCN2A | Sodium channel protein type 2 subunit alpha, is a protein that in humans is encoded by the SCN2A gene. Functional sodium channels contain an ion conductive alpha subunit and one or more regulatory beta subunits. Sodium channels which contain sodium channel protein type 2 subunit alpha are sometimes called Nav1.2 channels.
Function
Voltage-gated sodium channels are transmembrane glycoprotein complexes composed of a large alpha subunit with four domains including 24 transmembrane segments and one or more regulatory beta subunits. They are responsible for the generation and propagation of action potentials in neurons and muscle. This gene encodes one member of the sodium channel alpha subunit gene family. It is heterogeneously expressed in the brain, and mutations in this gene have been linked to several seizure disorders. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.
Clinical significance
Mutations in this gene have been implicated in cases of autism, infantile spasms, bitemporal glucose hypometabolism, and bipolar disorder.
See also
paralytic - SCN2A ortholog in Drosophila
References
Further reading
External links
Patient Organizations
The SCN2A Foundation
SCN2A Asia Pacific
SCN2A Germany e. V.
Sodium channels |
https://en.wikipedia.org/wiki/SH3GL2 | Endophilin-A1 is a protein that in humans is encoded by the SH3GL2 gene.
Interactions
SH3GL2 has been shown to interact with DNM1, Amphiphysin, ADAM9, SH3KBP1 and ADAM15.
References
Further reading |
https://en.wikipedia.org/wiki/SLAMF1 | Signaling lymphocytic activation molecule 1 is a protein that in humans is encoded by the SLAMF1 gene. Recently SLAMF1 has also been designated CD150 (cluster of differentiation 150).
SLAMF1 belongs to the signaling lymphocytic activation molecule family. The interaction of SLAMF1 promoter and enhancers with the Early B-cell factor 1 (EBF1) is required for the expression of SLAMF1 gene in B cells. STAT6, IRF4, and NF-kB factors involved in the transfer of the signals from the B-cell receptor, its co-receptors and IL-4R, also play important role in the regulation of SLAMF1 expression.
Interactions
SLAMF1 has been shown to interact with PTPN11, SH2D1A and SH2D1B.
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/Anion%20exchange%20protein%202 | Anion exchange protein 2 (AE2) is a membrane transport protein that in humans is encoded by the SLC4A2 gene. AE2 is functionally similar to the Band 3 Cl−/HCO3− exchange protein.
Mice have been used to explore the function of AE2. AE2 contributes to basolateral membrane HCO3− transport in the gastrointestinal tract. AE2 is required for spermiogenesis in mice. AE2 is required for normal osteoclast function. The activity of AE2 is sensitive to pH.
AE3 has been suggested as a target for prevention of diabetic vasculopathy.
Structure
The cryo electron microsopic studies revealed that human AE2 protein forms a homodimer and stays in resting state of inward-facing conformation at physiological pH. A loop between transmembrane (TM) helices 10 and 11 extends from TM domain into its cytoplamic domain, forming a "trigger" locking the TM helices in the resting state. In addition, the C-terminal loop (CTD loop) inserts into the anion binding pocket to further block its activities.
Mechanism of ion exchange
During the process of acid secretion, the cellular pH increases, triggering the release of the "trigger" loop from the cytoplasmic domain. This allows for the re-arrangement of the TM helices, while the CTD loop is forced out, enabling HCO3- binding. Further conformational changes then turn the AE2 protein into an outward-facing conformation, releasing HCO3- into the extracellular environment and capturing Cl- into the binding pocket. Finally, the AE2 protein returns to its inwar |
https://en.wikipedia.org/wiki/Small%20nuclear%20ribonucleoprotein%20polypeptide%20A | U1 small nuclear ribonucleoprotein A is a protein that in humans is encoded by the SNRPA gene.
Interactions
Small nuclear ribonucleoprotein polypeptide A has been shown to interact with CDC5L.
References
Further reading |
https://en.wikipedia.org/wiki/STC1 | Stanniocalcin-1 is a glycoprotein, a homologue of a hormone stanniocalcin, first discovered in bony fishes. In humans it is encoded by the STC1 gene.
Function
This gene encodes a secreted, homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The only known molecular function of human Stanniocalcin-1 to date is a SUMO E3 ubiquitin ligase activity in the SUMOylation cycle. However, STC1 interacts with many proteins in the cytoplasm, mitochondria, endoplasmatic reticulum, and in dot-like fashion in the cell nucleus. The N-terminal region of STC1 is the function region which is responsible to establish the interaction with its partners, including SUMO1. Low-resolution studies shows that STC1 is an anti-parallel homodimer in solution and the cysteine 202 is responsible for its dimerization. All the 5 disulfide bonds of human STC1 are conserved and have the same profile of fish STC. The gene contains a 5' UTR rich in CAG trinucleotide repeats. The encoded protein contains 11 conserved cysteine residues and is phosphorylated by protein kinase C exclusively on its serine residues.
The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Overexpression of human stanniocalcin 1 in mice produces high serum phosphate levels, dwarfism, and increased metabolic rate. This gene has altered expression in hepatocellular, |
https://en.wikipedia.org/wiki/TCF12 | Transcription factor 12 is a protein that in humans is encoded by the TCF12 gene.
The protein encoded by this gene is a member of the basic helix-loop-helix (bHLH) E-protein family that recognizes the consensus binding site (E-box) CANNTG. This encoded protein is expressed in many tissues, among them skeletal muscle, thymus, B- and T-cells, and may participate in regulating lineage-specific gene expression through the formation of heterodimers with other bHLH E-proteins. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined. TCF12 has been speculatively related to human male sexuality through a GWAS study indicating association to a related single nucleotide polymorphism. Mutations in this gene have also been associated with cases of coronal craniosynostosis.
TCF12 is the primary heterodimerising partner of TCF21, a tumour suppressor gene and a target of SRY/SOX9 activity.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Translin | Translin is a DNA-binding protein that in humans is encoded by the TSN gene. Together with translin-associated factor X, translin forms the component 3 of promoter of RISC (C3PO) complex which facilitates endonucleolytic cleavage of the passenger strand during microRNA loading into the RNA-induced silencing complex (RISC).
Function
This gene encodes a DNA-binding protein which specifically recognizes conserved target sequences at the breakpoint junction of chromosomal translocations. Translin polypeptides form a multimeric structure that is responsible for its DNA-binding activity. Recombination-associated motifs and translin-binding sites are present at recombination hotspots and may serve as indicators of breakpoints in genes which are fused by translocations. These binding activities may play a crucial role in chromosomal translocation in lymphoid neoplasms.
Interactions
Translin has been shown to interact with PPP1R15A.
References
Further reading
External links |
https://en.wikipedia.org/wiki/ZBTB17 | Zinc finger and BTB domain-containing protein 17 is a protein that in humans is encoded by the ZBTB17 gene.
Interactions
ZBTB17 has been shown to interact with TOPBP1, Host cell factor C1 and Myc.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/PRDM2 | PR domain zinc finger protein 2 is a protein that in humans is encoded by the PRDM2 gene.
Function
This tumor suppressor gene is a member of a nuclear histone/protein methyltransferase superfamily. It encodes a zinc finger protein that can bind to retinoblastoma protein, estrogen receptor, and the TPA-responsive element (MTE) of the heme-oxygenase-1 gene. Although the functions of this protein have not been fully characterized, it may (1) play a role in transcriptional regulation during neuronal differentiation and pathogenesis of retinoblastoma, (2) act as a transcriptional activator of the heme-oxygenase-1 gene, and (3) be a specific effector of estrogen action. Three transcript variants encoding different isoforms have been found for this gene.
Interactions
PRDM2 has been shown to interact with Estrogen receptor alpha and Retinoblastoma protein.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/HIST2H2AA3 | Histone H2A type 2-A is a protein that in humans is encoded by the HIST2H2AA3 gene.
Function
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the centromeric copy.
References
Further reading |
https://en.wikipedia.org/wiki/HIST1H2BG | Histone H2B type 1-C/E/F/G/I is a protein that in humans is encoded by the HIST1H2BG gene.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H2B family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.
References
Further reading |
https://en.wikipedia.org/wiki/PEA15 | Astrocytic phosphoprotein PEA-15 is a protein that in humans is encoded by the PEA15 gene.
PEA15 is a death effector domain (DED)-containing protein predominantly expressed in the central nervous system, particularly in astrocytes.
PEA-15 promotes autophagy in glioma cells in a JNK-dependent manner.
Interactions
PEA15 has been shown to interact with:
Caspase 8,
FADD, and
MAPK1,
Phospholipase D1, and
RPS6KA3.
References
Further reading |
https://en.wikipedia.org/wiki/ADAM9 | Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ADAM9 gene.
Function
This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene interacts with SH3 domain-containing proteins, binds mitotic arrest deficient 2 beta protein, and is also involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. Two alternative splice variants have been identified, encoding distinct isoforms.
Interactions
ADAM9 has been shown to interact with:
MAD2L2,
SH3GL2, and
SNX9
References
Further reading
External links
ADAM9 on the Atlas of Genetics and Oncology
Proteases
EC 3.4.24 |
https://en.wikipedia.org/wiki/SCYE1 | Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 is a protein that in humans is encoded by the AIMP1 gene.
The protein encoded by this gene is a cytokine that may be induced by apoptosis and is also released from professional antigen-presenting cells such as dendritic cells. The release of this cytokine renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor of SCYE1 (pro-SCYE1) is identical to the p43 subunit, which is associated with the multiaminoacyl-tRNA synthetase complex (mARS). Pro-SCYE1 may function in binding RNA as part of the tRNA synthetase complex in normal cells and in stimulating inflammatory responses after proteolytic cleavage in tumor cells. As an inflammatory cytokine, AIMp1/p43 has demonstrated the ability to skew T-helper polarization in the direction of Th-1, and its homozygous deletion leads to a hyper-polarized Th-2 phenotype.
Interactions
SCYE1 has been shown to interact with SMURF2.
References
Further reading |
https://en.wikipedia.org/wiki/CYTH2 | Cytohesin-2 is a protein that in humans is encoded by the CYTH2 gene.
Function
Cytohesin-2 (CYTH2), formerly known as Pleckstrin homology, Sec7 and coiled/coil domains 2 (PSCD2), is a member of the cytohesin family. Members of this family have identical structural organization that consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain. The coiled-coil motif is involved in homodimerization, the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity, and the PH domain interacts with phospholipids and is responsible for association of CYTHs with membranes. Members of this family appear to mediate the regulation of protein sorting and membrane trafficking. CYTH2 exhibits GEP activity in vitro with ARF1, ARF3, and ARF6. CYTH2 protein is 83% homologous to CYTH1. Two transcript variants encoding different isoforms have been found for this gene.
Interactions
CYTH2 has been shown to interact with Arrestin beta 2 and Arrestin beta 1.
References
Further reading |
https://en.wikipedia.org/wiki/COPS2 | COP9 signalosome complex subunit 2 is a protein that in humans is encoded by the COPS2 gene. It encodes a subunit of the COP9 signalosome.
Interactions
COPS2 has been shown to interact with:
DAX1,
IRF8,
NIF3L1, and
THRA.
References
External links
Further reading |
https://en.wikipedia.org/wiki/PRDX6 | Peroxiredoxin-6 is a protein that in humans is encoded by the PRDX6 gene. It is a member of the peroxiredoxin family of antioxidant enzymes.
Function
The protein encoded by this gene is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.
Model organisms
Model organisms have been used in the study of PRDX6 function. A conditional knockout mouse line, called Prdx6tm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty five tests were carried out on mutant mice but no significant abnormalities were observed.
References
Further reading
Genes mutated in mice
EC 1.11.1
EC 3.1.1 |
https://en.wikipedia.org/wiki/MDC1 | Mediator of DNA damage checkpoint protein 1 is a 2080 amino acid long protein that in humans is encoded by the MDC1 gene located on the short arm (p) of chromosome 6. MDC1 protein is a regulator of the Intra-S phase and the G2/M cell cycle checkpoints and recruits repair proteins to the site of DNA damage. It is involved in determining cell survival fate in association with tumor suppressor protein p53.
This protein also goes by the name Nuclear Factor with BRCT Domain 1 (NFBD1).
Function
Role in DNA damage response
The MDC1 gene encodes the MDC1 nuclear protein which is part of the DNA damage response (DDR) pathway, the mechanism through which eukaryotic cells respond to damaged DNA, specifically DNA double-strand breaks (DSB) that are caused by ionizing radiation or chemical clastogens. The DDR of mammalian cells is made up of kinases, and mediator/adaptors factors. In mammalian cells the DDR is a network of pathways made up of proteins that function as either kinases, or and mediator/adaptors that recruit the kinases to their phosphorylation targets, these factors work together to detect DNA damage, and signal the repair mechanism as well as activating cell cycle checkpoints. The MDC1s role in DDR is to function both as a mediator/adaptor protein mediating a complex of other DDR proteins at the site of DNA damage and repairing DNA damage through its PST domain.
When a cell is exposed to ionizing radiation, its chromatin can be damaged with DSB, triggering the DDR whi |
https://en.wikipedia.org/wiki/SRA1 | Steroid receptor RNA activator 1 also known as steroid receptor RNA activator protein (SRAP) is a protein that in humans is encoded by the SRA1 gene. The mRNA transcribed from the SRA1 gene is a component of the ribonucleoprotein complex containing NCOA1. This functional RNA also encodes a protein.
Function
This gene is involved in transcriptional coactivation by steroid receptor. There is currently data suggesting this gene encodes both a non-coding RNA that functions as part of a ribonucleoprotein complex and a protein coding mRNA. Increased expression of both the transcript and the protein is associated with cancer.
Interactions
SRA1 has been shown to interact with:
Estrogen receptor alpha,
DDX17,
Nuclear receptor coactivator 2, and
SPEN.
The SRAP has been shown to interact with its SRA RNA counterpart indirectly with the functional sub-structure STR7 of SRA RNA. Originally proposed to be RRM containing, SRAP has been demonstrated to have a helix bundle at its C-terminal end while N-terminal to this domain appears unstructured.
References
Further reading
External links |
https://en.wikipedia.org/wiki/ABCG5 | ATP-binding cassette sub-family G member 5 is a protein that in humans is encoded by the ABCG5 gene.
Function
The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. The protein encoded by this gene functions as a half-transporter to limit intestinal absorption and promote biliary excretion of sterols. It is expressed in a tissue-specific manner in the liver, colon, and intestine. This gene is tandemly arrayed on chromosome 2, in a head-to-head orientation with family member ABCG8. Mutations in this gene may contribute to sterol accumulation and atherosclerosis, and have been observed in patients with sitosterolemia.
Interactive pathway map
See also
ABCG5 and ABCG8 Genes
References
Further reading
External links
ATP-binding cassette transporters |
https://en.wikipedia.org/wiki/Allograft%20inflammatory%20factor%201 | Allograft inflammatory factor 1 (AIF-1) also known as ionized calcium-binding adapter molecule 1 (IBA1) is a protein that in humans is encoded by the AIF1 gene.
Gene
The AIF1 gene is located within a segment of the major histocompatibility complex class III region. It has been shown that this gene is highly expressed in testis, spleen, and brain but weakly expressed in lung, and kidney. Among brain cells, the Iba1 gene is strongly and specifically expressed in microglia. Circulating macrophages also express Iba1.
Function
AIF1 is a protein that exists in the cytoplasm, and it is highly evolutionarily conserved. It is also possibly identical to three other proteins, Iba-2, MRF-1 (microglia response factor) and daintain. However complete functional profiles of all three proteins and how they overlap is unknown. IBA1 is a 17-kDa EF hand protein that is specifically expressed in macrophages / microglia and is upregulated during the activation of these cells. Iba1 expression is up-regulated in microglia following nerve injury, central nervous system ischemia, and several other brain diseases.
AIF1 was originally discovered in atherosclerotic lesions in a rat model of chronic allograft cardiac rejection. It was found to be upregulated in macrophages and neutrophils in response to the cytokine IFN-γ. AIF1 expression has been seen to increase in vascular tissue in response to arterial injury, specifically it is found in activated vascular smooth muscle cells in response to IFN |
https://en.wikipedia.org/wiki/AMY2A | Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene.
Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the pancreas.
References
External links
See also
AMY1A
Further reading |
https://en.wikipedia.org/wiki/APOBEC1 | Apolipoprotein B mRNA editing enzyme, catalytic polypeptide 1 also known as C->U-editing enzyme APOBEC-1 is a protein that in humans is encoded by the APOBEC1 gene.
This gene encodes a member of the APOBEC protein family and the cytidine deaminase enzyme family. The encoded protein forms a multiple-protein RNA editing holoenzyme with APOBEC1 complementation factor (A1CF). This holoenzyme is involved in the editing of cytosine-to-uracil (C-to-U) nucleotide bases in apolipoprotein B and neurofibromin 1 mRNAs.
APOBEC-1 (A1) has been linked with cholesterol control, cancer development and inhibition of viral replication. Its function relies on introducing a stop codon into apolipoprotein B (ApoB) mRNA, which alters lipid metabolism in the gastrointestinal tract. The editing mechanism is highly specific. A1’s deamination of the cytosine base yields uracil, which creates a stop codon in the mRNA.
A1 has been linked with both positive and negative health effects. In rodents, it has wide tissue distribution where as in humans, it is only expressed in the small intestine.
Gene
APOBEC1 lies on human chromosome 12.
Function
ApoB is essential in the assembly of very low density lipoproteins from lipids, in the liver and small intestine. By editing ApoB, it forces only the smaller product, ApoB48, to be expressed, which greatly inhibits lipoprotein production. However, A1 is currently found only at extremely low levels in the human liver and intestine, while it is highly expres |
https://en.wikipedia.org/wiki/CHD3 | Chromodomain-helicase-DNA-binding protein 3 is an enzyme that in humans is encoded by the CHD3 gene.
Function
This gene encodes a member of the CHD family of proteins which are characterized by the presence of chromo (chromatin organization modifier) domains and SNF2-related helicase/ATPase domains. This protein is one of the components of a histone deacetylase complex referred to as the Mi-2/NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromatin remodeling is essential for many processes including transcription. Autoantibodies against this protein are found in a subset of patients with dermatomyositis. Three alternatively spliced transcripts encoding different isoforms have been described.
Mutations in CHD3 cause a neurodevelopmental syndrome (Snijders Blok-Campeau syndrome) with macrocephaly and impaired speech and language.
Interactions
CHD3 has been shown to interact with:
HDAC1,
Histone deacetylase 2 and
SERBP1.
References
External links
Further reading |
https://en.wikipedia.org/wiki/Contactin%201 | Contactin 1, also known as CNTN1, is a protein which in humans is encoded by the CNTN1 gene.
Function
The protein encoded by this gene is a member of the immunoglobulin superfamily. It is a glycosylphosphatidylinositol (GPI)-anchored neuronal membrane protein that functions as a cell adhesion molecule. It may play a role in the formation of axon connections in the developing nervous system. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.
Interactions
CNTN1 has been shown to interact with PTPRB.
References
External links
Further reading |
https://en.wikipedia.org/wiki/CRX%20%28gene%29 | Cone-rod homeobox protein is a protein that in humans is encoded by the CRX gene.
Function
The protein encoded by this gene is a photoreceptor-specific transcription factor which plays a role in the differentiation of photoreceptor cells. This homeodomain protein is necessary for the maintenance of normal cone and rod function. Mutations in this gene are associated with photoreceptor degeneration, Leber's congenital amaurosis type III and the autosomal dominant cone-rod dystrophy 2. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some variants has not been determined.
Mammalian CRX encodes a 299 amino acid protein containing a DNA binding homeodomain (HD) near its N-terminus followed by glutamine rich (Gln), and basic amino acid regions, then a C-terminal transactivation domain (AD). While structural biochemistry has demonstrated that the CRX HD adopts a canonical homeodomain protein fold, the AD is predicted to be flexible and disordered. The structural attributes of the CRX AD have yet to be solved.
Evolution
CRX is a divergent duplicate of OTX produced during the 2 rounds of vertebrate whole genome duplication.
In the eutherian mammals, CRX has again duplicated by tandem gene duplication, with six ancestral duplicates, which are collectively referred to as ETCHbox genes.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Retinitis Pigmentosa Overview
Transcription fa |
https://en.wikipedia.org/wiki/CRYBB2 | Beta-crystallin B2 is a protein that in humans is encoded by the CRYBB2 gene.
Function
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-terminal 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, is part of a gene cluster with beta-A4, beta-B1, and beta-B3. A chain-terminating mutation was found to cause type 2 cerulean cataracts.
Interactions
CRYBB2 has been shown to interact with Hsp27, CRYGC, CRYAA and CRYAB.
References
External links
Further reading |
https://en.wikipedia.org/wiki/CYP2J2 | Cytochrome P450 2J2 (CYP2J2) is a protein that in humans is encoded by the CYP2J2 gene. CYP2J2 is a member of the cytochrome P450 superfamily of enzymes. The enzymes are oxygenases which catalyze many reactions involved in the metabolism of drugs and other xenobiotics) as well as in the synthesis of cholesterol, steroids and other lipids.
Protein structure
The CYP2J2 contains the following domains:
• Hydrophobic binding domains
• F-G loop (containing non-conservative mutations) primary membrane binding motif
The protein also contains an N-terminal anchor.
F-G loop
The F-G loop mediates the binding and passage of substrates, and its hydrophobic region containing residues Trp-235, Phe-239 and Ille-236 allows the enzyme to interact with cellular membranes. Mutations to hydrophilic residues in the F-G loop alter the binding mechanism by changing insertion depth of the enzyme into the membrane.
Tissue distribution
CYP2J2 is expressed predominately in the heart and, to a lesser extent, in other tissues such as the liver, gastrointestinal tract, pancreas, lung, and central nervous system.
Function
CYP2J2 localizes to the endoplasmic reticulum and is thought to be a prominent enzyme responsible for metabolizing endogenous polyunsaturated fatty acids to signaling molecules. It metabolizes arachidonic acid to the following eicosatrienoic acid epoxides (termed EETs): 5,6-epoxy-8Z,11Z,14Z-EET, 8,9-epoxy-8Z,11Z,14Z-EET, 11,12-epoxy-5Z,8Z,14Z-EET, and 14,15-epoxy-5Z,8Z,11Z |
https://en.wikipedia.org/wiki/TIMM8A | Mitochondrial import inner membrane translocase subunit Tim8 A, also known as deafness-dystonia peptide or protein is an enzyme that in humans is encoded by the TIMM8A gene. This translocase has similarity to yeast mitochondrial proteins that are involved in the import of metabolite transporters from the cytoplasm into the mitochondrial inner membrane. The gene is mutated in deafness-dystonia syndrome (or Mohr-Tranebjaerg syndrome; MTS/DFN-1) and it is postulated that MTS/DFN-1 is a mitochondrial disease caused by a defective mitochondrial protein import system.
Structure
The TIMM8A gene is located on q arm of chromosome X in position 22.1 and spans 3,313 base pairs. The gene produces an 11 kDa protein composed of 97 amino acids. The structure shows resemblance to yeast translocase of the inner membrane (TIM) proteins with two conserved paired cysteine residue motifs. The cysteine residues organize zinc ions for stability and control other interactions with proteins.
Function
The human TIMM8A gene codes for a translocase involved in the import and insertion of hydrophobic membrane proteins from the cytoplasm into the mitochondrial inner membrane. It is also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. It acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 |
https://en.wikipedia.org/wiki/EEF2 | Eukaryotic elongation factor 2 is a protein that in humans is encoded by the EEF2 gene. It is the archaeal and eukaryotic counterpart of bacterial EF-G.
This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the ribosome. This protein is completely inactivated by EF-2 kinase phosphorylation.
aEF2/eEF2 found in most archaea and eukaryotes, including humans, contains a post translationally modified histidine diphthamide. It is the target of diphtheria toxin (from Corynebacterium diphtheriae), and exotoxin A (from Pseudomonas aeruginosa). The inactivation of EF-2 by toxins inhibits protein production in the host, causing symptoms due to loss of function in affected cells.
References
Further reading
External links |
https://en.wikipedia.org/wiki/EPH%20receptor%20A3 | EPH receptor A3 (ephrin type-A receptor 3) is a protein that in humans is encoded by the EPHA3 gene.
Function
This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene encodes a protein that binds ephrin-A ligands. Two alternatively spliced transcript variants have been described for this gene.
Interactions
EPH receptor A3 has been shown to interact with EFNB2 and EFNA5.
References
Further reading
Tyrosine kinase receptors |
https://en.wikipedia.org/wiki/FNTB | Protein farnesyltransferase subunit beta is an enzyme that in humans is encoded by the FNTB gene.
References
Further reading
External links |
https://en.wikipedia.org/wiki/GRK5 | G protein-coupled receptor kinase 5 is a member of the G protein-coupled receptor kinase subfamily of the Ser/Thr protein kinases, and is most highly similar to GRK4 and GRK6. The protein phosphorylates the activated forms of G protein-coupled receptors to regulate their signaling.
Function
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 phosphorylated, active receptor prevents receptor stimulation of heterotrimeric G protein transducer proteins, blocking their cellular signaling and resulting in receptor desensitization. Arrestin binding also directs receptors to specific cellular internalization pathways, removing the receptors from the cell surface and also preventing additional activation. Arrestin binding to phosphorylated, active receptor also enables receptor signaling through arrestin partner proteins. Thus the GRK/arrestin system serves as a complex signaling switch for G protein-coupled receptors.
GRK5 and the closely related GRK6 phosphorylate receptors at sites that encourage arrestin-mediated signaling rather than arrestin-mediated receptor desensitization, internalization and trafficking (in contrast to GRK2 and GRK3, which have the opposite effect). This difference is one basis for pharmacological biased agonism (also called functional selectivity), where a drug binding to a receptor may bias that receptor’s signaling toward a parti |
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