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Description:
PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
Description:
The pantothenate kinase (PANK) family of proteins catalyzes the first step in coenzyme A (CoA) biosynthesis. Coenzyme A is an important coenzyme involved in the synthesis and oxidation of fatty acids, as well as the oxidation of pyruvate in the citric acid (Krebs) cycle. Pantothenate kinase 3 (PANK3) is a 370 amino acid member of the pantothenate kinase family that plays a role in the physiological regulation of the intracellular CoA concentration. Localized to the cytoplasm, PANK3 is regulated by feedback inhibition by CoA and its thioesters. PANK3 transfers a phosphate from ATP to pantothenate (Vitamin B5), resulting in formation of 4’-phosphopantothenate. Closely related to its family members, PANK1, PANK2 and PANK4, PANK3 is highly expressed in liver. Pantothenate kinase associated neurodegeneration (PKAN) results from mutations in the gene encoding PANK2, the only mitochondria targeted human PANK.
Description:
The protein encoded by this gene binds nucleosomal DNA and is associated with transcriptionally active chromatin. Along with a similar protein, HMG17, the encoded protein may help maintain an open chromatin configuration around transcribable genes.
Description:
TWIST1 and TWIST2 are basic helix-loop-helix transcriptional repressors that bind to E boxes in gene promoters, acting as master regulators in a variety of biological processes, including organogenesis, osteogenesis, cancer progression and hematopoietic cell development. Both TWIST1 and TWIST2 are found to act as Homodimers or Heterodimers with another bHLH protein. TWIST1 Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. TWIST1 also represses expression of proinflammatory cytokines such as TNFA and IL1B. TWIST2 inhibits transcriptional activation by MYOD1, MYOG, MEF2A, and MEF2C. Twist2 inhibits the premature or ectopic differentiation of preosteoblast cells during osteogenesis.
Description:
Twist2 (Twist homolog 2) is a basic helix-loop-helix (bHLH) transcription factor which acts as a transcriptional repressor. It binds to the E-box consensus sequence 5'-CANNTG-3' and inhibits transcriptional activation by MYOD1, MYOG, MEF2A and MEF2C. Efficient DNA binding requires dimerization with another bHLH protein. Twist2 inhibits the premature or ectopic differentiation of preosteoblast cells during osteogenesis.
Description:
Twist2 (Twist homolog 2) is a basic helix-loop-helix (bHLH) transcription factor which acts as a transcriptional repressor. It binds to the E-box consensus sequence 5'-CANNTG-3' and inhibits transcriptional activation by MYOD1, MYOG, MEF2A and MEF2C. Efficient DNA binding requires dimerization with another bHLH protein. Twist2 inhibits the premature or ectopic differentiation of preosteoblast cells during osteogenesis.
Description:
DSCR1 protein influences cardiac and nervous system development (1). DSCR1 is abundant in the brain, heart, and skeletal muscle. Overexpression of DSCR1 may play a role in the pathogenesis of Down syndrome, in particular mental retardation and/or cardiac defects. DSCR1 inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Human DSCR1 maps to gene locus 21q22.1-q22.2.
Description:
DSCR1 protein influences cardiac and nervous system development (1). DSCR1 is abundant in the brain, heart, and skeletal muscle. Overexpression of DSCR1 may play a role in the pathogenesis of Down syndrome, in particular mental retardation and/or cardiac defects. DSCR1 inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Human DSCR1 maps to gene locus 21q22.1-q22.2.
Description:
Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. In Saccharomyces cerevisiae, ubiquitin-like proteins include Rub1, Ula1, Uba3, Smt3, Ubc2, Ubc12 and Ubc9. Rub1 shares 53% homology with ubiquitin and requires activation via the E2 proteins, including Ula1, Uba3 and Ubc12 in order to conjugate to substrates directed to different proteolytic systems. Ubc4 catalyzes ubiquitination of IkBa in a phosphorylation and SCFB-TRCP dependent manner. In this particular reaction, E1 first transfers ubiquitin to the E2 component Ubc4, and Ubc4 then associates with E3 ligase, which conjugates the poly-ubiquitin chain on a target protein. In this fashion, the chain tags the IkBa for degradation by a proteasome thus lifting the inhibitory effect of IkBa on NFkB and allowing NFkB to enter the nucleus.
Description:
UBE2H, also known as UBC8, UBCH, UBCH2 or E2-20K, is a 183 amino acid protein involved in ubiquitin-mediated protein degradation. Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). One of several members of the ubiquitin-conjugating enzyme family, UBE2H functions as an E2 ubiquitin-conjugating enzyme that acts to catalyze the covalent attachment of ubiquitin residues to various proteins, including Histone H2A. UBE2H shares 100% identity with its mouse counterpart and 98% identity with its frog and zebrafish homologs, suggesting a conserved function between species. Multiple isoforms of UBE2H exist due to alternative splicing events.
Description:
UBE2H, also known as UBC8, UBCH, UBCH2 or E2-20K, is a 183 amino acid protein involved in ubiquitin-mediated protein degradation. Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). One of several members of the ubiquitin-conjugating enzyme family, UBE2H functions as an E2 ubiquitin-conjugating enzyme that acts to catalyze the covalent attachment of ubiquitin residues to various proteins, including Histone H2A. UBE2H shares 100% identity with its mouse counterpart and 98% identity with its frog and zebrafish homologs, suggesting a conserved function between species. Multiple isoforms of UBE2H exist due to alternative splicing events.
Description:
MAVS (Mitochondrial Antiviral Signaling) mediates the activation of NF-kappaB and IRF3 in response to antiviral infection. Silencing of MAVS expression permits derepression of viral replication, while over expression of MAVS boosts antiviral immunity.
Description:
MAVS (Mitochondrial Antiviral Signaling) mediates the activation of NF-kappaB and IRF3 in response to antiviral infection. Silencing of MAVS expression permits derepression of viral replication, while over expression of MAVS boosts antiviral immunity.
Description:
Three highly similar proteins termed NOMO1, NOMO2 and NOMO3, are encoded by a gene mapping to a region of duplication on the p arm of human chromosome 16. All three NOMO proteins share similar functions and have been difficult to characterize individually. NOMO1 (Nodal modulator 1), also known as PM5, is a 1,222 amino acid highly conserved single-pass type I membrane protein expressed in colon tumor tissue and normal colonic mucosa. NOMO proteins are novel antagonists of Nodal signaling which interact with Nicalin to form a Nicalin-NOMO complex, and are rapidly degraded or stabilized by Nicalin. NOMO proteins were once considered candidates for the development of pseudoxanthoma elasticum (PXE), a heritable disorder of connective tissue, as the NOMO genes are located in close proximity to the gene responsible for PXE development (MRP6).
Description:
Three highly similar proteins termed NOMO1, NOMO2 and NOMO3, are encoded by a gene mapping to a region of duplication on the p arm of human chromosome 16. All three NOMO proteins share similar functions and have been difficult to characterize individually. NOMO1 (Nodal modulator 1), also known as PM5, is a 1,222 amino acid highly conserved single-pass type I membrane protein expressed in colon tumor tissue and normal colonic mucosa. NOMO proteins are novel antagonists of Nodal signaling which interact with Nicalin to form a Nicalin-NOMO complex, and are rapidly degraded or stabilized by Nicalin. NOMO proteins were once considered candidates for the development of pseudoxanthoma elasticum (PXE), a heritable disorder of connective tissue, as the NOMO genes are located in close proximity to the gene responsible for PXE development (MRP6).
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