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Description:
The assembly of very-low-density lipoproteins (VLDLs) in the secretory apparatus of the hepatocyte relies on the mobilization of triacylglycerol (TAG) from the cytosolic pool by lipolysis and re-esterification. However, some of the re-esterified TAG products are returned to the cytosolic pool in the liver, which protects vulnerable body tissues from excess lipotoxic non-esterified fatty acids in the plasma. Some of the lipases involved in this process include arylacetamide deacetylase (AADAC) and its related proteins AADACL1 and AADACL2. AADAC, a single pass type II membrane protein of the endoplasmic reticulum, is expressed in hepatocytes, intestinal mucosal cells, pancreas and adrenal gland. It plays an important role in the metabolic activation of arylamine substrates to ultimate carcinogens. AADACL1 hydrolyzes the metabolic intermediate 2-acetyl monoalkylglycerol, and its inactivation results in disruption of ether lipid metabolism in cancer cells and impaired cell migration and tumor growth.
Description:
Barrier-to-autointegration factor (BAF) binds non-specifically to double stranded DNA, possibly to play a role in tissue- or cell type-specific gene expression by interacting with different homeodomain transcription factors. BAF compresses chromatin structure and interacts with the LEM domain of nuclear proteins to play a crucial role in membrane recruitment and chromatin decondensation during nuclear assembly. Additionally, retroviruses like HIV-1 incorporate BAF from host cells into preintegration complexes (PICs) to prevent autointegration of retroviral DNA and thereby promote integration of retroviral DNA into the host chromosome.
Description:
Phosphatidate phosphatases are a family of integral membrane glycoproteins that dephosphorylate a variety of lipid phosphates and play a role in signal transduction via the phospholipase D pathway. PAP-2 proteins function independently of Mg2+ and are insensitive to NEM (N-ethylmaleimide) inhibition. The lipid phosphates degraded by this family include ceramide 1-phosphate (C1P), sphingosine 1-phosphate (S1P), phosphatidic acid (PA) and lysophosphatidic acid (LPA). LPPR4 (lipid phosphate phosphatase-related protein type 4), also known as LPR4, PHP1, PRG1 or PRG-1, is a 763 amino acid multi-pass membrane protein that belongs to the PA-phosphatase related phosphoesterase family. Exclusively expressed in neurons, LPPR4 hydrolyzes lysophosphatidic acid (LPA) and facilitates axonal outgrowth during development and regenerative sprouting. LPPR4 exists as two alternatively spliced isoforms and is encoded by a gene located on human chromosome 1p21.2.
Description:
KLF7 is a transcriptional activator that belongs to the Krüppel C2H2-type zinc finger protein family. KLF7 targets promotor regions bearing CACCC elements in order to regulate transcription. It is believed that KLF7 is an important element for regulation of differentiation and the development of nervous systems. Specifically, increased expression of KLF7 is associated with neuronal precursors exiting the cell cycle and beginning to differentiate. Overexpression of KLF7 can lead to cell cycle arrest and a decrease in DNA synthesis. Also, KLF7 is thought to regulate the expression of Trk A, the receptor for nerve growth factor, which is required for the normal growth and maturation of neurons. KLF7 is a widely expressed protein with highest expression found in brain and nervous tissue.
Description:
Velis are a family of small synaptic proteins that interact with other proteins at the post-synaptic density (PSD) of neuronal synapses. Velis contain the PDZ motif involved in recruiting cell adhesion molecules, receptors, and channels. Veli1 (also designated Lin-7A and MALS-1), Veli2 (also designated Lin-7B and MALS-2), and Veli3 (also designated Lin-7C and MALS-3) are mammalian homologs of C. elegans LIN-7. Veli proteins are ubiquitously expressed with high expression in brain, liver, and testis. Velis are localized at the synaptic junctions in neurons. Velis bind to CASK, a neurexin-binding protein highly concentrated in synapses, and Mint1, a binding partner with a vesicle trafficking protein.
Description:
MAGOH, the human homolog of Drosophila mago nashi, is required for embryo development. MAGOH is ubiquitously expressed in adult tissues. It has an unusual structure consiting of an extremely flat, six-stranded anti-parallel β sheet packed next to two helices. MAGOH interacts with the Y14 protein to form a complex that plays a crucial role in postsplicing processing (including nuclear export and cytoplasmic localization of the mRNA) and in the nonsense-mediated mRNA decay (NMD) surveillance process. The MAGOH-Y14 complex remains persistently associated in the same position on the mRNA after its export to the cytoplasm and requires translation of the mRNA for removal. This complex may illustrate the mechanism of the pre-mRNA splicing machinery for forming a stable exon-exon junction complex-mRNA at splice junctions.
Description:
The SWI/SNF complex regulates gene expression via ATP-dependent chromatin remodeling. Brm (SNF2-a), Brg-1 (SNF2-b), Ini1 (integrase interactor 1, SNF5), BAF53 (ARPn beta), BAF57, BAF155 (SRG3), and BAF170 make up the functional core. BAF53 homologues from yeast to humans contain a conserved N-terminal motif, which contains residues at serine 2 and tyrosine 6, which play important roles in BAF53 activity. The BAF53 protein shuttles between the nucleus and cytoplasm. BAF53 also forms a complex with TIP49 and TIP48, which mediates c-Myc oncogenic activity.
Description:
Regulator of histone methyltransferase complexes that plays an essential role in embryonic development, including heart and liver development, neural tube fusion process and hematopoiesis. Acts by modulating histone methyltransferase activity and promoting the recruitment of histone methyltransferase complexes to their target genes. Binds DNA and mediates the recruitment of the PRC2 complex to target genes in embryonic stem cells. Does not have histone demethylase activity but regulates activity of various histone methyltransferase complexes. In embryonic stem cells, it associates with the PRC2 complex and inhibits trimethylation of 'Lys-27' of histone H3 (H3K27me3) by the PRC2 complex, thereby playing a key role in differentiation of embryonic stem cells and normal development. In cardiac cells, it is required to repress expression of cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases. Also acts as a transcriptional repressor of ANF via its interaction with GATA4 and NKX2-5. Participates in the negative regulation of cell proliferation signaling.
Description:
Hox, Pbx and Meis families of transcription factors form heteromeric complexes and bind DNA through specific homeobox domains. Hox proteins are involved in regulating tissue patterning during development, and are also expressed in lineage- and stage-specific patterns during adult hematopoietic differentiation and in leukemias. The Hox proteins, which include paralog groups 1-10, have a low intrinsic binding affinity for DNA and are instead associated into cooperative DNA binding complexes with Pbx or the Pbx- related Meis proteins, which result in an enhanced Hox-DNA binding affinity and an increased selectivity for the binding site. Both Meis1 and Meis2 (also known as Meis-related gene 1 or Mrg1) are members of the TALE (“three amino acid loop extensionâ€) family of homeodomain-containing proteins. In addition to binding with Hox proteins, Meis1 also forms heterodimers with the ubiquitously expressed Pbx proteins, including Pbx1, Pbx2 and Pbx3, and these complexes contain distinct DNA-binding specificities. Like Hox and Pbx proteins, Meis1 is implicated in oncogenesis, as it is overexpressed as a result of adjacent retroviral insertion in BHX-2 myeloid leukemias. Two Meis-related proteins, Meis2 and Meis3 (also designated Mrg1 and Mrg2, respectively), possess largely similar sequence identity with Meis1 and are expressed in normal tissues and myeloid leukemias. In the pancreas, Meis2 preferentially associates with Pbx1, and together they associate with the pancreas-specific homeodomain factor, Pdx1, to repress Pdx1-induced transcriptional activation.
Description:
p21-activated kinases (PAKs) belong to the family of serine/threonine kinases involved in the control of various cellular processes, including the cell cycle, dynamics of the cytoskeleton, apoptosis, oncogenic transformation, and transcription. All PAK family members are characterized by the presence of p21-binding domain. p21-activated kinases are regulated by the small GTP-binding proteins Rac and Cdc42, and lipids, which stimulate autophosphorylation and phosphorylation of exogenous substrates. Serine (Ser-474) is the likely autophosphorylation site in the kinase domain of PAK4 in vivo. Phosphospecific directed against serine 474 detect activated PAK4 on the Golgi membrane when PAK4 is co-expressed with activated Cdc42. Current data strongly implicates PAK-4 in oncogenesis. PAK4 is frequently overexpressed in human tumor cell lines of various tissue origins.
Description:
Synapsin II is a member of the synapsin gene family. Synapsins are neuronal phosphoproteins which associate with the cytoplasmic surface of synaptic vesicles. Family members are characterized by common protein domains, and they are implicated in synaptogenesis and the modulation of neurotransmitter release, suggesting a potential role in several neuropsychiatric diseases. This member of the synapsin family is a neuron-specific phosphoprotein that selectively binds to small synaptic vesicles in the presynaptic nerve terminal.
Description:
The amphoterin-induced gene and ORF (AMIGO) family of proteins consists of AMIGO1, AMIGO2 and AMIGO3. All three members are single pass type I membrane proteins that contain several leucine-rich repeats, one IgG domain, and a transmembrane domain. The AMIGO proteins are specifically expressed on fiber tracts of neuronal tissues and participate in their formation. The AMIGO proteins can form complexes with each other, but can also bind itself. AMIGO1, also designated Alivin-2, promotes growth and fasciculation of neurites and plays a role in myelination and fasciculation of developing neural axons. In cerebellar neurons, AMIGO2 (Alivin-1) is crucial for depolarization-dependent survival. Similar to AMIGO1 and AMIGO2, AMIGO3 (Alivin-3) plays a role in homophilic and/or heterophilic cell-cell interaction and signal transduction.
Description:
The protein encoded by this gene is a tetraspanin protein that is thought to be involved in WNT signaling. Defects in this gene are a cause of Joubert syndrome-14. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012].
Description:
ANKRD28 selectively inhibits the phosphatase activity of PPP1C and targets PPP1C to modulate HNRPK phosphorylation. It contains twenty seven ANK repeats. There are two named isoforms.
Description:
This gene encodes a protein that interacts with the forkhead-associated domain of the Ki-67 antigen. The encoded protein may bind RNA and may play a role in mitosis and cell cycle progression. Multiple pseudogenes exist on chromosomes 5, 10, 12, 15, and 19.[provided by RefSeq, Jan 2009].
UOM:
1 * 100 µl
Promotion
,BOSSBS-7937REA
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