3229 Results for: "ACTIVE MOTIF"

Supplier: Bioss

Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (1–3). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (1–3). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).

Supplier: Bioss

This is a paternally expressed imprinted gene that encodes transcripts containing two overlapping open reading frames (ORFs), RF1 and RF1/RF2, as well as retroviral-like slippage and pseudoknot elements, which can induce a -1 nucleotide frame-shift. ORF1 encodes a shorter isoform with a CCHC-type zinc finger motif containing a sequence characteristic of gag proteins of most retroviruses and some retrotransposons. The longer isoform is the result of -1 translational frame-shifting leading to translation of a gag/pol-like protein combining RF1 and RF2. It contains the active-site consensus sequence of the protease domain of pol proteins. Additional isoforms resulting from alternatively spliced transcript variants, as well as from use of upstream non-AUG (CUG) start codon, have been reported for this gene. Increased expression of this gene is associated with hepatocellular carcinomas. [provided by RefSeq, May 2010].

Supplier: Bioss

Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (13). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (13). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).

Supplier: Bioss

ADAMTS (A Disintegrin And Metalloproteinase Domain with Thrombospondin type 1 Modules) is a family of zinc-dependent proteases that are implicated in a variety of normal and pathological conditions, including arthritis and cancer. ADAMTS protein family members contain an amino-terminal propeptide domain, a metalloproteinase domain, a disintegrin-like domain and a carboxy-terminus that contains a varying number of Thrombospondin type 1 (TSP-1) motifs. ADAMTS-L2 (ADAMTS-like protein 2) is a 951 amino acid secreted protein that is highly expressed in lung, kidney and liver. Mutations in the gene encoding ADAMTS are the cause of geleophysic dysplasia, an autosomal recessive disorder characterized by cardiac vavular anomalies, short stature, thick skin and brachydactyly. In individuals affected with geleophysic dysplasia, there is a significant increase in total active TGF-beta 1 and nuclear locations of p-SAMD2 in fibroblasts. Interestingly, ADAMTS-L2 interacts with LTBP-1, a glycoprotein that is part of the platelet-derived TGF-beta 1 complex.

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).

Supplier: Bioss

Acts as a transcriptional activator or repressor. Involved in embryonic lens fiber cell development. Recruits the transcriptional coactivators CREBBP and/or EP300 to crystallin promoters leading to up-regulation of crystallin gene during lens fiber cell differentiation. Activates the expression of IL4 in T helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis by interacting with MYB and decreasing BCL2 expression. Together with PAX6, transactivates strongly the glucagon gene promoter through the G1 element. Activates transcription of the CD13 proximal promoter in endothelial cells. Represses transcription of the CD13 promoter in early stages of myelopoiesis by affecting the ETS1 and MYB cooperative interaction. Involved in the initial chondrocyte terminal differentiation and the disappearance of hypertrophic chondrocytes during endochondral bone development. Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf response element) sites of lens-specific alpha- and beta-crystallin gene promoters. Binds element G1 on the glucagon promoter. Binds an AT-rich region adjacent to the TGC motif (atypical Maf response element) in the CD13 proximal promoter in endothelial cells (By similarity). When overexpressed, represses anti-oxidant response element (ARE)-mediated transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Binds to the ARE sites of detoxifying enzyme gene promoters.

Supplier: Bioss

p130 represents one of several known substrates for v-Crk encoded p47. p130 Cas (for Crk-associated substrate) exhibits a high level of tyrosine phosphorylation and is tightly associated with v-Crk, suggesting a role in v-Crk-mediated cell Signalling. The molecular cloning of p130 Cas has shown it to represent a novel SH3 containing Signalling molecule with a cluster of multiple putative SH2-binding motifs for v-Crk. By immunoprecipitation analysis, p130 Cas has been shown to be highly phosphorylated at tyrosine residues subsequent to either v-Src p60 or v-Crk-mediated transformation and to form stable complexes with both of these transforming proteins. p130 Cas behaves as an extremely potent substrate for protein tyrosine kinases and has been reported to relocate from the cytoplasm to cell membrane upon tyrosine phosphorylation. One proposed model is that the SH2 domain of v-Crk functions to activate c-Src kinase, which in turn phosphorylates p130 Cas.

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. 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. ZNRF1 (zinc and ring finger 1), also known as NIN283, is a 227 amino acid protein that contains one RING-type zinc finger and localizes to the lysosome and the endosome, as well as to cytoplasmic vesicles and the peripheral membrane. Expressed primarily in nervous system tissue, but also present in testis and thymus, ZNRF1 functions as an E3 ubiquitin-protein ligase that is thought to play a role in the establishment and maintenance of neuronal plasticity. Multiple isoforms of ZNRF1 exist due to alternative splicing events.

Supplier: Bioss

p130 represents one of several known substrates for v-Crk encoded p47. p130 Cas (for Crk-associated substrate) exhibits a high level of tyrosine phosphorylation and is tightly associated with v-Crk, suggesting a role in v-Crk-mediated cell signaling. The molecular cloning of p130 Cas has shown it to represent a novel SH3 containing signaling molecule with a cluster of multiple putative SH2-binding motifs for v-Crk. By immunoprecipitation analysis, p130 Cas has been shown to be highly phosphorylated at tyrosine residues subsequent to either v-Src p60 or v-Crk-mediated transformation and to form stable complexes with both of these transforming proteins. p130 Cas behaves as an extremely potent substrate for protein tyrosine kinases and has been reported to relocate from the cytoplasm to cell membrane upon tyrosine phosphorylation. One proposed model is that the SH2 domain of v-Crk functions to activate c-Src kinase, which in turn phosphorylates p130 Cas.

Supplier: Bioss

p130 represents one of several known substrates for v-Crk encoded p47. p130 Cas (for Crk-associated substrate) exhibits a high level of tyrosine phosphorylation and is tightly associated with v-Crk, suggesting a role in v-Crk-mediated cell signaling. The molecular cloning of p130 Cas has shown it to represent a novel SH3 containing signaling molecule with a cluster of multiple putative SH2-binding motifs for v-Crk. By immunoprecipitation analysis, p130 Cas has been shown to be highly phosphorylated at tyrosine residues subsequent to either v-Src p60 or v-Crk-mediated transformation and to form stable complexes with both of these transforming proteins. p130 Cas behaves as an extremely potent substrate for protein tyrosine kinases and has been reported to relocate from the cytoplasm to cell membrane upon tyrosine phosphorylation. One proposed model is that the SH2 domain of v-Crk functions to activate c-Src kinase, which in turn phosphorylates p130 Cas.

Supplier: Bioss

PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.

Supplier: Bioss

PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.

Supplier: Bioss

PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.

Supplier: Bioss

This gene encodes a member of the estrogen receptor-related receptor (ESRR) family, which belongs to the nuclear hormone receptor superfamily. All members of the ESRR family share an almost identical DNA binding domain, which is composed of two C4-type zinc finger motifs. The ESRR members are orphan nuclear receptors; they bind to the estrogen response element and steroidogenic factor 1 response element, and activate genes controlled by both response elements in the absence of any ligands. The ESRR family is closely related to the estrogen receptor (ER) family. They share target genes, co-regulators and promoters, and by targeting the same set of genes, the ESRRs seem to interfere with the ER-mediated estrogen response in various ways. It has been reported that the family member encoded by this gene functions as a transcriptional activator of DNA cytosine-5-methyltransferases 1 (Dnmt1) expression by direct binding to its response elements in the DNMT1 promoters, modulates cell proliferation and estrogen signaling in breast cancer, and negatively regulates bone morphogenetic protein 2-induced osteoblast differentiation and bone formation. Multiple alternatively spliced transcript variants have been identified, which mainly differ at the 5' end and some of which encode protein isoforms differing in the N-terminal region.

Supplier: Bioss

PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.

Supplier: Bioss

WD-repeats are motifs that are found in a variety of proteins and are characterised by a conserved core of 40-60 amino acids that commonly form a tertiary propeller structure. While proteins that contain WD-repeats participate in a wide range of cellular functions, they are generally involved in regulatory mechanisms concerning chromatin assembly, cell cycle control, signal transduction, RNA processing, apoptosis and vesicular trafficking. WDFY1 positively regulates TLR3- and TLR4-mediated signaling pathways by bridging the interaction between TLR3 or TLR4 and TICAM1. WDFY1 Promotes TLR3/4 ligand-induced activation of transcription factors IRF3 and NF-kappa-B, as well as the production of IFN-beta and inflammatory cytokines. WDFY2 acts in an adapter protein-like fashion to mediate the interaction between the kinase PRKCZ and its substrate VAMP2 and increases the PRKCZ-dependent phosphorylation of VAMP2. WDFY2 positively regulates adipocyte differentiation, by facilitating the phosphorylation and thus inactivation of the anti-adipogenetic transcription factor FOXO1 by the kinase AKT1.

Supplier: Bioss

Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterised by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.

Supplier: Bioss

Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.

Supplier: Bioss

MTA1 is a component of the NURD (nucleosome remodeling and histone deacetylation) complex, which is associated with ATP-dependent chromatin-remodeling and histone deacetylase activity. MTA1 functions in conjunction with other components of NURD to mediate transcriptional repression as it facilitates the association of repressor molecules with the chromatin. Structurally, MTA1 contains a single SH3-binding motif and a zinc finger domain, along with a region similar to the co-repressor protein N-Cor. MTA1 is normally expressed at low levels in various tissues and is more highly expressed in testis. Overexpression of MTA1 correlates with tumor invasion and metastasis in various carcinomas including colorectal, gastrointestinal and breast carcinomas. Elevation of MTA1 levels in these tumors appears to enhance the metastases to lymph nodes, increase mammary cell motility and potentiate growth, and therefore may be an indicator for assessing the potential malignancies of various tumors. A similar protein, MTA2, also designated MTA1-L1 (MTA1-like protein 1), shares more than 55% sequence homology with MTA1 and is ubiquitously expressed.

Supplier: Bioss

MTA1 is a component of the NURD (nucleosome remodeling and histone deacetylation) complex, which is associated with ATP-dependent chromatin-remodeling and histone deacetylase activity. MTA1 functions in conjunction with other components of NURD to mediate transcriptional repression as it facilitates the association of repressor molecules with the chromatin. Structurally, MTA1 contains a single SH3-binding motif and a zinc finger domain, along with a region similar to the co-repressor protein N-Cor. MTA1 is normally expressed at low levels in various tissues and is more highly expressed in testis. Overexpression of MTA1 correlates with tumor invasion and metastasis in various carcinomas including colorectal, gastrointestinal and breast carcinomas. Elevation of MTA1 levels in these tumors appears to enhance the metastases to lymph nodes, increase mammary cell motility and potentiate growth, and therefore may be an indicator for assessing the potential malignancies of various tumors. A similar protein, MTA2, also designated MTA1-L1 (MTA1-like protein 1), shares more than 55% sequence homology with MTA1 and is ubiquitously expressed.

Supplier: Bioss

MTA1 is a component of the NURD (nucleosome remodeling and histone deacetylation) complex, which is associated with ATP-dependent chromatin-remodeling and histone deacetylase activity. MTA1 functions in conjunction with other components of NURD to mediate transcriptional repression as it facilitates the association of repressor molecules with the chromatin. Structurally, MTA1 contains a single SH3-binding motif and a zinc finger domain, along with a region similar to the co-repressor protein N-Cor. MTA1 is normally expressed at low levels in various tissues and is more highly expressed in testis. Overexpression of MTA1 correlates with tumor invasion and metastasis in various carcinomas including colorectal, gastrointestinal and breast carcinomas. Elevation of MTA1 levels in these tumors appears to enhance the metastases to lymph nodes, increase mammary cell motility and potentiate growth, and therefore may be an indicator for assessing the potential malignancies of various tumors. A similar protein, MTA2, also designated MTA1-L1 (MTA1-like protein 1), shares more than 55% sequence homology with MTA1 and is ubiquitously expressed.

Supplier: Bioss

Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (1–3). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (1–3). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).

Supplier: Bioss

ADAMTS (A Disintegrin And Metalloproteinase Domain with Thrombospondin type 1 Modules) is a family of zinc-dependent proteases that are implicated in a variety of normal and pathological conditions, including arthritis and cancer. ADAMTS protein family members contain an amino-terminal propeptide domain, a metalloproteinase domain, a disintegrin-like domain and a carboxy-terminus that contains a varying number of Thrombospondin type 1 (TSP-1) motifs. ADAMTS-L2 (ADAMTS-like protein 2) is a 951 amino acid secreted protein that is highly expressed in lung, kidney and liver. Mutations in the gene encoding ADAMTS are the cause of geleophysic dysplasia, an autosomal recessive disorder characterised by cardiac vavular anomalies, short stature, thick skin and brachydactyly. In individuals affected with geleophysic dysplasia, there is a significant increase in total active TGF-beta 1 and nuclear locations of p-SAMD2 in fibroblasts. Interestingly, ADAMTS-L2 interacts with LTBP-1, a glycoprotein that is part of the platelet-derived TGF-beta 1 complex.

Supplier: Bioss

Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of cellular differentiation, immunity, peripheral circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively. Recruits distinct combinations of cofactors to target gene regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates the circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-selective manner. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as ARNTL/BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORC-mediated activation of the expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism, including PLIN2 and AVPR1A. Negative regulator of adipocyte differentiation through the regulation of early phase genes expression, such as MMP3. Controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. In liver, has specific and redundant functions with RORA as positive or negative modulator of expression of genes encoding phase I and Phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as SULT1E1.

Supplier: Bioss

Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of cellular differentiation, immunity, peripheral circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively. Recruits distinct combinations of cofactors to target gene regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates the circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-selective manner. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as ARNTL/BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORC-mediated activation of the expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism, including PLIN2 and AVPR1A. Negative regulator of adipocyte differentiation through the regulation of early phase genes expression, such as MMP3. Controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. In liver, has specific and redundant functions with RORA as positive or negative modulator of expression of genes encoding phase I and Phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as SULT1E1.

Supplier: Bioss

p130 represents one of several known substrates for v-Crk encoded p47. p130 Cas (for Crk-associated substrate) exhibits a high level of tyrosine phosphorylation and is tightly associated with v-Crk, suggesting a role in v-Crk-mediated cell signaling. The molecular cloning of p130 Cas has shown it to represent a novel SH3 containing signaling molecule with a cluster of multiple putative SH2-binding motifs for v-Crk. By immunoprecipitation analysis, p130 Cas has been shown to be highly phosphorylated at tyrosine residues subsequent to either v-Src p60 or v-Crk-mediated transformation and to form stable complexes with both of these transforming proteins. p130 Cas behaves as an extremely potent substrate for protein tyrosine kinases and has been reported to relocate from the cytoplasm to cell membrane upon tyrosine phosphorylation. One proposed model is that the SH2 domain of v-Crk functions to activate c-Src kinase, which in turn phosphorylates p130 Cas.

Supplier: Bioss

p130 represents one of several known substrates for v-Crk encoded p47. p130 Cas (for Crk-associated substrate) exhibits a high level of tyrosine phosphorylation and is tightly associated with v-Crk, suggesting a role in v-Crk-mediated cell signaling. The molecular cloning of p130 Cas has shown it to represent a novel SH3 containing signaling molecule with a cluster of multiple putative SH2-binding motifs for v-Crk. By immunoprecipitation analysis, p130 Cas has been shown to be highly phosphorylated at tyrosine residues subsequent to either v-Src p60 or v-Crk-mediated transformation and to form stable complexes with both of these transforming proteins. p130 Cas behaves as an extremely potent substrate for protein tyrosine kinases and has been reported to relocate from the cytoplasm to cell membrane upon tyrosine phosphorylation. One proposed model is that the SH2 domain of v-Crk functions to activate c-Src kinase, which in turn phosphorylates p130 Cas.

Supplier: Bioss

ADAMTS proteases are secreted enzymes containing a prometalloprotease domain of the reprolysin type. The ADAMTS proteases function in processing of procollagens and von Willebrand factor as well as catabolism of aggrecan, versican and brevican. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration.A member of the metalloproteinase family containing disintegrin like domains (ADAMs), the function of ADAMTS8 is still poorly understood. ADAMTS8 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active on a range of substrates. ADAMTS8 is inhibited by the endogenous MMP inhibitors, TIMP1, 2, 3 and 4, but most efficiently by TIMP3. In addition to the metalloprotease domain, ADAMTS8 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine rich domain and thrombospondin 1 like domains.

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. 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. ZNRF1 (zinc and ring finger 1), also known as NIN283, is a 227 amino acid protein that contains one RING-type zinc finger and localizes to the lysosome and the endosome, as well as to cytoplasmic vesicles and the peripheral membrane. Expressed primarily in nervous system tissue, but also present in testis and thymus, ZNRF1 functions as an E3 ubiquitin-protein ligase that is thought to play a role in the establishment and maintenance of neuronal plasticity. Multiple isoforms of ZNRF1 exist due to alternative splicing events.

Supplier: Bioss

Sorting nexin (SNX) proteins are members of a large family of hydrophilic PX (phospholipid-binding motif) domain-containing proteins that interact with a variety of receptor types. SNXs are widely expressed, although the tissue distribution of each SNX mRNA varies. The ability of SNXs to bind specific phospholipids, as well as their tendency to form protein-protein complexes, suggests a role for these proteins in cellular membrane trafficking and protein sorting. SNXs may also function specifically in pro-degradative sorting, internalization, endosomal recycling or simply in endosomal sorting. SNXs partially associate with cellular membranes, despite their hydrophilic nature. SNX9 resides in the cytosol where it influences the processing and trafficking of insulin receptors. The enzyme aldolase binds to and inactivates SNX9. Phosphorylation of SNX9 releases aldolase and frees SNX9 to recruit and activate Dynamin II, a neuronal phosphoprotein and a GTPase enzyme which mediates late stages of endocytosis in both neural and non-neural cells.