"Bioss"

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IGKV A18.

Supplier: Bioss

The protein encoded by this gene is a preproprotein that is proteolytically processed to form the secreted opioid peptides beta-neoendorphin, dynorphin, leu-enkephalin, rimorphin, and leumorphin. These peptides are ligands for the kappa-type of opioid receptor. Dynorphin is involved in modulating responses to several psychoactive substances, including cocaine. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2010].

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GNG2 (Guanine nucleotide binding protein (G protein), gamma 2) is a member of the guanine nucleotide-binding proteins (G proteins) family. Heterotrimeric G proteins are involved as a modulator or transducer in various transmembrane signaling systems. The specificity of a G protein-receptor interaction is primarily mediated by the gamma subunit.

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Breast cancer metastasis-suppressor 1 (BRMS1) is 246 amino acid protein that acts as a mediator of metastasis suppression in several types of cancer including ovarian, lung, bladder, and murine mammary. BRMS1 mRNA is expressed in various tissues, including ovary, prostate, testis, and colon, but the protein is primarily detected in term placenta. BRMS1 suppresses metastasis without inhibiting tumorigenicity by modifying several metastasis-associated phenotypes. BRMS1 may participate in transcriptional regulation by binding to the mSin3/histone deacetylase complex. The expression of BRMS1 in certain cells increases connexin Cx43 expression and reduces connexin Cx32 expression. This produces a gap junction that increases intercellular communication, similar to those found in normal breast tissue. BRMS1 is stabilized by Hsp90 and may inhibit NF-â…¹B activity.

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Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates to mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor.

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This gene encodes a member of the semicarbazide-sensitive amine oxidase family. Copper amine oxidases catalyze the oxidative conversion of amines to aldehydes in the presence of copper and quinone cofactor. The encoded protein is localized to the cell surface, has adhesive properties as well as monoamine oxidase activity, and may be involved in leukocyte trafficking. Alterations in levels of the encoded protein may be associated with many diseases, including diabetes mellitus. A pseudogene of this gene has been described and is located approximately 9-kb downstream on the same chromosome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2013]

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Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.

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ATG4A is a cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.

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AKT, also known as protein kinase B (PKB), is a 57 kDa serine/threonine protein kinase. There are three mammalian isoforms of Akt: AKT1 (PKB alpha), AKT2 (PKB beta) and AKT3 (PKB gamma) with AKT2 and AKT3 being approximately 82% identical with the AKT1 isoform. Each isoform has a pleckstrin homology (PH)domain, a kinase domain and a carboxy terminal regulatory domain. AKT was originally cloned from the retrovirus AKT8, and is a key regulator of many signal transduction pathways. Its tight control over cell proliferation and cell viability are manifold; overexpression or inappropriate activation of AKT has been seen in many types of cancer. AKT mediates many of the downstream events of phosphatidylinositol 3 kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI3 kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus.

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The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF135 (RING finger protein 135), also known as L13, is a 432 amino acid protein that contains one RING-type zinc finger and one SPRY domain. Via its RING-type zinc finger, RNF135 may play a role in transcriptional regulation and protein degradation events. Defects in the gene encoding RNF135 are the cause of RNF135-related overgrowth syndrome which is characterized by learning disabilities, facial dysmorphism and increased weight and height. Multiple isoforms of RNF135 exist due to alternative splicing events.

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Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5.

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CDC-like kinase 2 (CLK2) belongs to a family of autophosphorylating kinases termed CLK (CDC2/CDC28-like kinases), which have been shown to phosphorylate serine- and arginine-rich (SR) proteins of the spliceosomal complex, and to influence alternative splicing in overexpression systems. Recent findings demonstrated that the CLK kinases activate PTP-1B family members, and this phosphatase may be an important cellular target for CLK action. Mutations in the CLK2 proteins affect organismal features such as development, behavior, reproduction, and aging as well as cellular features such as the cell cycle, apoptosis, the DNA replication checkpoint, and telomere length.

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Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signaling. Has no interleukin-1 like activity.

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UGP2 (UDP glucose pyrophosphorylase 2) is an important intermediary in cellular metabolic pathways. It transfers a glucose moiety from glucose-1-phosphate to MgUTP and forms UDP glucose and MgPPi.

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Plays a major role in tight junction-specific obliteration of the intercellular space.

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CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.