44064 Results for: "Bioss"

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This gene is a member of the peptidase C19 family and encodes a protein that is similar to ubiquitin-specific proteases. Though this gene is located on the X chromosome, it escapes X-inactivation. Mutations in this gene have been associated with Turner syndrome. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

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This gene is a member of the peptidase C19 family and encodes a protein that is similar to ubiquitin-specific proteases. Though this gene is located on the X chromosome, it escapes X-inactivation. Mutations in this gene have been associated with Turner syndrome. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

Supplier: Bioss

The RING finger motif is a specialized DNA-binding zinc finger domain found in many transcriptional regulatory proteins. The ring finger protein (RNF) family includes any protein containing the signature RING finger motif. RNF186 (RING finger protein 186) is a 227 amino acid multi-pass membrane protein containing one RING-type zinc finger. The gene encoding RNF186 maps to human chromosome 1p36.13. Chromosome 1 is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1. Notably, the rare aging disease Hutchinson-Gilford progeria is associated with the LMNA gene which encodes lamin A. The MUTYH gene is located on chromosome 1 and is partially responsible for familial adenomatous polyposis. Stickler syndrome, Parkinsons, Gaucher disease and Usher syndrome are also associated with chromosome 1.

Supplier: Bioss

The RING finger motif is a specialized DNA-binding zinc finger domain found in many transcriptional regulatory proteins. The ring finger protein (RNF) family includes any protein containing the signature RING finger motif. RNF186 (RING finger protein 186) is a 227 amino acid multi-pass membrane protein containing one RING-type zinc finger. The gene encoding RNF186 maps to human chromosome 1p36.13. Chromosome 1 is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1. Notably, the rare aging disease Hutchinson-Gilford progeria is associated with the LMNA gene which encodes lamin A. The MUTYH gene is located on chromosome 1 and is partially responsible for familial adenomatous polyposis. Stickler syndrome, Parkinsons, Gaucher disease and Usher syndrome are also associated with chromosome 1.

Supplier: Bioss

The RING finger motif is a specialized DNA-binding zinc finger domain found in many transcriptional regulatory proteins. The ring finger protein (RNF) family includes any protein containing the signature RING finger motif. RNF186 (RING finger protein 186) is a 227 amino acid multi-pass membrane protein containing one RING-type zinc finger. The gene encoding RNF186 maps to human chromosome 1p36.13. Chromosome 1 is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1. Notably, the rare aging disease Hutchinson-Gilford progeria is associated with the LMNA gene which encodes lamin A. The MUTYH gene is located on chromosome 1 and is partially responsible for familial adenomatous polyposis. Stickler syndrome, Parkinsons, Gaucher disease and Usher syndrome are also associated with chromosome 1.

Supplier: Bioss

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. RNF185 (ring finger protein 185), also known as FLJ38628, is a 192 amino acid multi-pass membrane protein containing one RING-type zinc finger. Two RNF185 isoforms exist as a result of alternative splicing, and the gene encoding RNF185 maps to human chromosome 22, which houses over 500 genes and is the second smallest human chromosome. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, Neurofibromatosis type 2, autism and schizophrenia.

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Ubiquitin is a highly conserved protein that is covalently linked to other proteins to regulate their function and degradation. This gene encodes a member of the ubiquitin-specific protease family of cysteine proteases. The enzyme specifically cleaves ubiquitin from ubiquitin-conjugated protein substrates. The protein is found in the nucleus and cytoplasm. It functions as a co-factor of the DNA-bound androgen receptor complex, and is inhibited by a protein in the Ras-GTPase pathway. The human genome contains several pseudogenes similar to this gene. Several transcript variants, some protein-coding and others not protein-coding, have been found for this gene. [provided by RefSeq, Jan 2013].

Supplier: Bioss

Provides, together with MAGI1, an adhesion machinery at tight junctions, which may regulate the permeability of kidney glomerulus and small intestinal epithelial cells. Mediates calcium-independent homophilic cell adhesion. In testis, it may function as a cell adhesion molecule rather than a tight-junction protein. It may participate in the adhesion between spermatogonia-spermatogonia, spermatogonia-Sertoli cells, and Sertoli cells-Sertoli cells.

Supplier: Bioss

Provides, together with MAGI1, an adhesion machinery at tight junctions, which may regulate the permeability of kidney glomerulus and small intestinal epithelial cells. Mediates calcium-independent homophilic cell adhesion. In testis, it may function as a cell adhesion molecule rather than a tight-junction protein. It may participate in the adhesion between spermatogonia-spermatogonia, spermatogonia-Sertoli cells, and Sertoli cells-Sertoli cells.

Supplier: Bioss

Provides, together with MAGI1, an adhesion machinery at tight junctions, which may regulate the permeability of kidney glomerulus and small intestinal epithelial cells. Mediates calcium-independent homophilic cell adhesion. In testis, it may function as a cell adhesion molecule rather than a tight-junction protein. It may participate in the adhesion between spermatogonia-spermatogonia, spermatogonia-Sertoli cells, and Sertoli cells-Sertoli cells.

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IGSF3, also known as V8 or EWI-3, is a 1,214 amino acid protein. Widely expressed with predominant expression in kidney, placenta and lung, IGSF3 localizes to the membrane and contains an N-terminal signal peptide, eight immunoglobulin (Ig) domains and a transmembrane segment. IGSF3 exhibits strong sequence and structural similarity to CD101 (32% identity), a leukocyte surface protein with seven Ig domains that is believed to play a role in T-cell activation. Despite the structural similarities between IGSF3 and CD101, IGSF3 is not expressed in peripheral blood lymphocytes and does not appear to participate in an immune function. Based on its subcellular localization and the presence of the eight Ig domains, IGSF3 is hypothesized to function as a surface receptor or as a cell adhesion molecule.

Supplier: Bioss

IGSF3, also known as V8 or EWI-3, is a 1,214 amino acid protein. Widely expressed with predominant expression in kidney, placenta and lung, IGSF3 localizes to the membrane and contains an N-terminal signal peptide, eight immunoglobulin (Ig) domains and a transmembrane segment. IGSF3 exhibits strong sequence and structural similarity to CD101 (32% identity), a leukocyte surface protein with seven Ig domains that is believed to play a role in T-cell activation. Despite the structural similarities between IGSF3 and CD101, IGSF3 is not expressed in peripheral blood lymphocytes and does not appear to participate in an immune function. Based on its subcellular localization and the presence of the eight Ig domains, IGSF3 is hypothesized to function as a surface receptor or as a cell adhesion molecule.

Supplier: Bioss

Involved in oxygen transport from the lung to the various peripheral tissues. LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure. Spinorphin: functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation.

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Essential ion channel and serine/threonine-protein kinase. Divalent cation channel permeable to calcium and magnesium. Has a central role in magnesium ion homeostasis and in the regulation of anoxic neuronal cell death. Involved in TNF-induced necroptosis downstream of MLKL by mediating calcium influx. The kinase activity is essential for the channel function. May be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1).

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Proteins containing PDZ domains have been shown frequently to bind the C-termini of transmembrane receptors or ion channels. They have also been shown to bind to other PDZ domain proteins and could possibly be involved in intracellular signalling. PDZK3 contains six PDZ domains and shares sequence similarity with pro-interleukin-16 (pro-IL-16). Like pro-IL-16, the encoded protein localizes to the endoplasmic reticulum and is thought to be cleaved by a caspase to produce a secreted peptide containing two PDZ domains. In addition, the PDZK3 gene is upregulated in primary prostate tumors and may be involved in the early stages of prostate tumorigenesis.

Supplier: Bioss

Involved in accumulation of zinc in synaptic vesicles.

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Diversin, also known as ANKRD6 (ankyrin repeat domain 6), is a 727 amino acid protein that contains eight ankyrin repeats and belongs to the ankyrin repeat domain protein family. Members of the ankyrin repeat domain family facilitate protein-protein interactions and function as adaptors of signaling pathways. Expressed in a developmentally-regulated manner and at highest levels in the brain, Diversin is believed to play a role in brain development. Via its ankyrin repeats, Diversin can directly interact with Dvl (dishevelled), an interaction that is essential for the activation of noncanonical Wnt signaling. In addition, Diversin contains a C-terminal domain that binds Axin/Conductin and a casein kinase-binding domain in its central region that specifically binds casein kinase Ié. Through the action of these additional domains, Diversin may also facilitate canonical Wnt signaling. Due to alternative splicing events, three Diversin isoforms exist.

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TTC33 contains 3 TPR repeats. The function of the TTC33 protein remains unknown.

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TTC33 contains 3 TPR repeats. The function of the TTC33 protein remains unknown.

Supplier: Bioss

E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.

Supplier: Bioss

Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus.

Supplier: Bioss

Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. ZSWIM3 (Zinc finger SWIM domain-containing protein 3) is a 696 amino acid protein that contains one SWIM-type zinc finger. SWIM domains are found in a variety of eukaryotic and prokaryotic proteins and are thought to be critical for certain ubiquitination reactions. The gene encoding ZSWIM3 maps to human chromosome 20, which contains nearly 63 million bases that encode over 600 genes, some of which are associated with Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome.

Supplier: Bioss

Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. ZSWIM3 (Zinc finger SWIM domain-containing protein 3) is a 696 amino acid protein that contains one SWIM-type zinc finger. SWIM domains are found in a variety of eukaryotic and prokaryotic proteins and are thought to be critical for certain ubiquitination reactions. The gene encoding ZSWIM3 maps to human chromosome 20, which contains nearly 63 million bases that encode over 600 genes, some of which are associated with Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome.

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Members of the suppressor of cytokine signaling (SOCS) family of proteins contain C-terminal regions of homology called the SOCS box, which serves to couple SOCS proteins and their binding partners with the Elongin B and C complex. Several other families of proteins also contain SOCS boxes, but differ from the SOCS proteins in the type of domain they contain upstream of the SOCS box. The largest family of SOCS box-containing proteins is the ankyrin repeat and SOCS box-containing (ASB) protein family. Members of the ASB family include ASB-1 through ASB-18 and are involved in a variety of biological processes. ASB-17 is a 295 amino acid member of this family. ASB-17 contains one ankyrin repeat and one SOCS box domain. ASB-17 is thought to be a substrate-recognition subunit of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin protein ligase complex. This complex mediates the ubiquitination of target proteins and their subsequent proteasomal degradation.

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RNF20 is an E3 ubiquitin ligase protein that mediates monoubiquitination of histone H2B and the methylation of histone H3. It forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBE2E1/UBCH6. It thereby plays a central role in histone code and gene regulation. It is required for transcriptional activation of Hox genes. It is recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator.

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Promotes neurite formation. Cooperates with PRDX1 to drive postmitotic motor neuron differentiation. The glycerophosphodiester phosphodiesterase activity may be required for its role in neuronal differentiation. May contribute to the osmotic regulation of cellular glycerophosphocholine.

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ZPI, also known as SERPINA10 (serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10) or PZI, is a 444 amino acid secreted protein that functions as a Protein Z-dependent protease inhibitor. Expressed by the liver, ZPI is secreted into the plasma where, in the presence of calcium, Protein Z and phospholipids, it inhibits the activated pro-coagulation factors X and XI (Factor X and Factor XI). This inhibition helps properly regulate intravenous blood clotting. ZPI, a member of the serpin protein family, contains five potential N-linked glycosylation sites and a tyrosine at position 387 which, when disrupted, renders ZPI inactive. Defects in the gene encoding ZPI may increase susceptibility to venous thrombosis, the formation of blood clots within a vein.

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SERPINB10 is a serine proteinase inhibitor of the ovalbumin like B clade of serpins. It was first discovered in human bone marrow in a search for serpins similar to SerpinB6. SERPINB10 was identified in lymphocytes, and was elevated in chronic myeloid leukemia and chronic myelomonocytic leukemia cells. The monocytic cell lines THP-1 and AML-193 also showed elevated SERPINB10 expression.

Supplier: Bioss

SERPINB10 is a serine proteinase inhibitor of the ovalbumin like B clade of serpins. It was first discovered in human bone marrow in a search for serpins similar to SerpinB6. SERPINB10 was identified in lymphocytes, and was elevated in chronic myeloid leukemia and chronic myelomonocytic leukemia cells. The monocytic cell lines THP-1 and AML-193 also showed elevated SERPINB10 expression.

Supplier: Bioss

Component of a probable SCF-like E3 ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably plays a role in the degradation of proteins involved in endothelial proliferation and/or differentiation (By similarity). Seems not to promote polyubiquitination and proteasomal degradation of TP53. In vitro, complexes of CUL7 with either CUL9 or FBXW8 or TP53 contain E3 ubiquitin-protein ligase activity.Involvement in disease: Defects in CUL7 are the cause of 3M syndrome type 1 (3M1). An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies.