Search results for DAO

Showing 18 results out of 20

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Protein (6 results from a total of 7)

DAO

Identifier: R-HSA-9033150
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: DAO: P14920

DAO

Identifier: R-HSA-389807
Species: Homo sapiens
Compartment: peroxisomal matrix
Primary external reference: UniProt: DAO: P14920
Identifier: R-HSA-5339682
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GSK3B: P49841
Identifier: R-HSA-9703308
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P41212
Identifier: R-HSA-9703306
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: Q92614
Identifier: R-HSA-9703314
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: Q92614

Complex (1 results from a total of 1)

Identifier: R-HSA-389849
Species: Homo sapiens
Compartment: peroxisomal matrix

Chemical Compound (1 results from a total of 1)

Identifier: R-ALL-159352
Compartment: cytosol
Primary external reference: ChEBI: dopamine 3-O-sulfate: 37946

Reaction (6 results from a total of 7)

Identifier: R-HSA-159358
Species: Homo sapiens
Compartment: cytosol
The catecholamine neurotransmitter dopamine (DA) is predominantly (>95%) conjugated with sulfate (dopamine 3-O-sulfate, DAOS) in human blood circulation. Human SULT1A3 and SULT1A4 are the major sulfotransferases that sulfonate DA (as well as other catecholamines and phenols) (Reiter et al. 1983, Johnson et al. 1980, Thomae et al. 2003, Hildebrandt et al. 2004).
Identifier: R-HSA-174446
Species: Homo sapiens
Compartment: nucleoplasm
The remaining flap, which is too short to support RPA binding, is then processed by FEN1. There is evidence that binding of RPA to the displaced end of the RNA-containing Okazaki fragment prevents FEN1 from accessing the substrate. FEN1 is a structure-specific endonuclease that cleaves near the base of the flap at a position one nucleotide into the annealed region. Biochemical studies have shown that the preferred substrate for FEN1 consists of a one-nucleotide 3'-tail on the upstream primer in addition to the 5'-flap of the downstream primer (Harrington and Lieber 1994, Harrington and Lieber 1995, Murante et al. 1996, Lieber 1997, Kaiser et al. 1999, Xu et al. 2000, Kao et al. 2002). The interaction of FEN1 with WRN, a RECQ family DNA helicase, is needed for successful flap cleavage during telomeric strand displacement synthesis (Saharia et al. 2010, Li et al. 2017).
Identifier: R-HSA-8944104
Species: Homo sapiens
Compartment: nucleoplasm, cytosol
PTEN (phosphatase and tensin homolog deleted in chromosome 10) is a tumor suppressor gene that is deleted or mutated in a variety of human cancers. TP53 (p53) stimulates PTEN transcription (Stambolic et al. 2000, Singh et al. 2002). PTEN, acting as a negative regulator of PI3K/AKT signaling, affects cell survival, cell cycling, proliferation and migration. PTEN regulates TP53 stability by inhibiting AKT-mediated activation of TP53 ubiquitin ligase MDM2, and thus enhances TP53 transcriptional activity and its own transcriptional activation by TP53. Beside their cross-regulation, PTEN and TP53 can interact and cooperate to regulate survival or apoptotic phenomena (Stambolic et al. 2000, Singh et al. 2002, Nakanishi et al. 2014).
In response to UV induced DNA damage, PTEN transcription is stimulated by binding of the transcription factor EGR1 to the promoter region of PTEN (Virolle et al. 2001).
PTEN transcription is also stimulated by binding of the activated nuclear receptor PPARG (PPARgamma) to peroxisome proliferator response elements (PPREs) in the promoter of the PTEN gene (Patel et al. 2001), binding of the ATF2 transcription factor, activated by stress kinases of the p38 MAPK family, to ATF response elements in the PTEN gene promoter (Shen et al. 2006) and by the transcription factor MAF1 (Li et al. 2016).
NR2E1 (TLX) associated with transcription repressors binds the evolutionarily conserved TLX consensus site in the PTEN promoter. NR2E1 inhibits PTEN transcription by associating with various transcriptional repressors, probably in a cell type or tissue specific manner. PTEN transcription is inhibited when NR2E1 forms a complex with ATN1 (atrophin-1) (Zhang et al. 2006, Yokoyama et al. 2008), KDM1A (LSD1) histone methyltransferase containing CoREST complex (Yokoyama et al. 2008), or histone deacetylases HDAC3, HDAC5 or HDAC7 (Sun et al. 2007).
Binding of the transcriptional repressor SNAI1 (Snail1) to the PTEN promoter represses PTEN transcription. SNAI1-mediated repression of PTEN transcription may require phosphorylation of SNAI1 on serine residue S246. Binding of SNAI1 to the PTEN promoter increases in response to ionizing radiation and is implicated in SNAI1-mediated resistance to gamma-radiation induced apoptosis (Escriva et al. 2008). Binding of another Slug/Snail family member SNAI2 (SLUG) to the PTEN gene promoter also represses PTEN transcription (Uygur et al. 2015).
Binding of JUN to the AP-1 element in the PTEN gene promoter (Hettinger et al. 2007) inhibits PTEN transcription. JUN partner FOS is not needed for JUN-mediated downregulation of PTEN (Vasudevan et al. 2007).
Binding of the transcription factor SALL4 to the PTEN gene promoter (Yang et al. 2008) and SALL4-medaited recruitment of the transcriptional repressor complex NuRD (Lu et al. 2009, Gao et al. 2013), containing histone deacetylases HDAC1 and HDAC2, inhibits the PTEN gene transcription. SALL4-mediated recruitment of DNA methyltransferases (DNMTs) is also implicated in transcriptional repression of PTEN (Yang et al. 2012).
Binding of the transcription factor MECOM (EVI1) to the PTEN gene promoter and MECOM-mediated recruitment of polycomb repressor complexes containing BMI1 (supposedly PRC1.4), and EZH2 (PRC2) leads to repression of PTEN transcription (Song et al. 2009, Yoshimi et al. 2011).
Identifier: R-HSA-5632993
Species: Homo sapiens
Compartment: nucleoplasm, cytosol
PTEN (phosphatase and tensin homolog deleted in chromosome 10) is a tumor suppressor gene that is deleted or mutated in a variety of human cancers. TP53 (p53) stimulates PTEN transcription (Stambolic et al. 2000, Singh et al. 2002). PTEN, acting as a negative regulator of PI3K/AKT signaling, affects cell survival, cell cycling, proliferation and migration. PTEN regulates TP53 stability by inhibiting AKT-mediated activation of TP53 ubiquitin ligase MDM2, and thus enhances TP53 transcriptional activity and its own transcriptional activation by TP53. Beside their cross-regulation, PTEN and TP53 can interact and cooperate to regulate survival or apoptotic phenomena (Stambolic et al. 2000, Singh et al. 2002, Nakanishi et al. 2014).
In response to UV induced DNA damage, PTEN transcription is stimulated by binding of the transcription factor EGR1 to the promoter region of PTEN (Virolle et al. 2001).
PTEN transcription is also stimulated by binding of the activated nuclear receptor PPARG (PPARgamma) to peroxisome proliferator response elements (PPREs) in the promoter of the PTEN gene (Patel et al. 2001), binding of the ATF2 transcription factor, activated by stress kinases of the p38 MAPK family, to ATF response elements in the PTEN gene promoter (Shen et al. 2006) and by the transcription factor MAF1 (Li et al. 2016).
NR2E1 (TLX) associated with transcription repressors binds the evolutionarily conserved TLX consensus site in the PTEN promoter. NR2E1 inhibits PTEN transcription by associating with various transcriptional repressors, probably in a cell type or tissue specific manner. PTEN transcription is inhibited when NR2E1 forms a complex with ATN1 (atrophin-1) (Zhang et al. 2006, Yokoyama et al. 2008), KDM1A (LSD1) histone methyltransferase containing CoREST complex (Yokoyama et al. 2008), or histone deacetylases HDAC3, HDAC5 or HDAC7 (Sun et al. 2007).
Binding of the transcriptional repressor SNAI1 (Snail1) to the PTEN promoter represses PTEN transcription. SNAI1-mediated repression of PTEN transcription may require phosphorylation of SNAI1 on serine residue S246. Binding of SNAI1 to the PTEN promoter increases in response to ionizing radiation and is implicated in SNAI1-mediated resistance to gamma-radiation induced apoptosis (Escriva et al. 2008). Binding of another Slug/Snail family member SNAI2 (SLUG) to the PTEN gene promoter also represses PTEN transcription (Uygur et al. 2015).
Binding of JUN to the AP-1 element in the PTEN gene promoter (Hettinger et al. 2007) inhibits PTEN transcription. JUN partner FOS is not needed for JUN-mediated downregulation of PTEN (Vasudevan et al. 2007).
Binding of the transcription factor SALL4 to the PTEN gene promoter (Yang et al. 2008) and SALL4-medaited recruitment of the transcriptional repressor complex NuRD (Lu et al. 2009, Gao et al. 2013), containing histone deacetylases HDAC1 and HDAC2, inhibits the PTEN gene transcription. SALL4-mediated recruitment of DNA methyltransferases (DNMTs) is also implicated in transcriptional repression of PTEN (Yang et al. 2012).
Binding of the transcription factor MECOM (EVI1) to the PTEN gene promoter and MECOM-mediated recruitment of polycomb repressor complexes containing BMI1 (supposedly PRC1.4), and EZH2 (PRC2) leads to repression of PTEN transcription (Song et al. 2009, Yoshimi et al. 2011).
Identifier: R-HSA-5339713
Species: Homo sapiens
Compartment: cytosol
GSK3beta mRNA is subject to aberrant splicing in stem cells in chronic myeloid leukemia. Missplicing leads to in-frame deletion of exons 8 and 9 which encode the FRAT and AXIN binding domains of the protein (Jamieson et al, 2008; Abrahamsson et al, 2009). Cells expressing the mutant GSK3beta have elevated levels of nuclear beta-catenin and high levels of TCF-dependent reporter activity (Jamieson et al, 2008; Abrahamsson et al, 2009). Although it is possible that the defect in the ability of mutant GSK3beta to promote beta-catenin degradation arises from an inability to bind to AXIN and form a functional degradation complex, this has not been formally demonstrated.
Identifier: R-HSA-9703433
Species: Homo sapiens
Compartment: cytosol
In addition to internal tandem duplications and activating point mutations, the FLT3 locus is also subject at low frequency to translocations (reviewed in Reiter and Gotlib, 2017; Kazi and Roonstrand, 2019). These translocations generally bring together an N-terminal partner gene encoding a dimerization domain with the intracellular portion of FLT3 containing the kinase domain and result in a protein that undergoes constitutive, ligand-independent dimerization. To date, 6 fusion partner genes have been identified: ETV6 (the most frequent), GOLGB1, SPTBN1, ZMYM2, TRIP11 and MYO18A, although not all have been functionally characterized. Where examined, the fusion proteins promote downstream signaling through the PI3K/AKT, MAP kinase and STAT5 signaling pathways and support IL-3-independent transformation of murine BaF3 cells (Baldwin et al, 2007; Vu et al, 2006; Vu et al, 2009; Walz et al, 2011; Falchi et al, 2014; Chung et al, 2017; Troadec et al, 2017; Grand et al, 2007; Jawhar et al, 2017; Zhang et al, 2018; Chonabayashi et al, 2013; reviewed in Kazi and Roonstrand, 2019).

Pathway (4 results from a total of 4)

Identifier: R-HSA-5628897
Species: Homo sapiens
While the p53 tumor suppressor protein (TP53) is known to inhibit cell growth by inducing apoptosis, senescence and cell cycle arrest, recent studies have found that p53 is also able to influence cell metabolism to prevent tumor development. TP53 regulates transcription of many genes involved in the metabolism of carbohydrates, nucleotides and amino acids, protein synthesis and aerobic respiration.

TP53 stimulates transcription of TIGAR, a D-fructose 2,6-bisphosphatase. TIGAR activity decreases glycolytic rate and lowers ROS (reactive oxygen species) levels in cells (Bensaad et al. 2006). TP53 may also negatively regulate the rate of glycolysis by inhibiting the expression of glucose transporters GLUT1, GLUT3 and GLUT4 (Kondoh et al. 2005, Schwartzenberg-Bar-Yoseph et al. 2004, Kawauchi et al. 2008).

TP53 negatively regulates several key points in PI3K/AKT signaling and downstream mTOR signaling, decreasing the rate of protein synthesis and, hence, cellular growth. TP53 directly stimulates transcription of the tumor suppressor PTEN, which acts to inhibit PI3K-mediated activation of AKT (Stambolic et al. 2001). TP53 stimulates transcription of sestrin genes, SESN1, SESN2, and SESN3 (Velasco-Miguel et al. 1999, Budanov et al. 2002, Brynczka et al. 2007). One of sestrin functions may be to reduce and reactivate overoxidized peroxiredoxin PRDX1, thereby reducing ROS levels (Budanov et al. 2004, Papadia et al. 2008, Essler et al. 2009). Another function of sestrins is to bind the activated AMPK complex and protect it from AKT-mediated inactivation. By enhancing AMPK activity, sestrins negatively regulate mTOR signaling (Budanov and Karin 2008, Cam et al. 2014). The expression of DDIT4 (REDD1), another negative regulator of mTOR signaling, is directly stimulated by TP63 and TP53. DDIT4 prevents AKT-mediated inactivation of TSC1:TSC2 complex, thus inhibiting mTOR cascade (Cam et al. 2014, Ellisen et al. 2002, DeYoung et al. 2008). TP53 may also be involved, directly or indirectly, in regulation of expression of other participants of PI3K/AKT/mTOR signaling, such as PIK3CA (Singh et al. 2002), TSC2 and AMPKB (Feng et al. 2007).

TP53 regulates mitochondrial metabolism through several routes. TP53 stimulates transcription of SCO2 gene, which encodes a mitochondrial cytochrome c oxidase assembly protein (Matoba et al. 2006). TP53 stimulates transcription of RRM2B gene, which encodes a subunit of the ribonucleotide reductase complex, responsible for the conversion of ribonucleotides to deoxyribonucleotides and essential for the maintenance of mitochondrial DNA content in the cell (Tanaka et al. 2000, Bourdon et al. 2007, Kulawiec et al. 2009). TP53 also transactivates mitochondrial transcription factor A (TFAM), a nuclear-encoded gene important for mitochondrial DNA (mtDNA) transcription and maintenance (Park et al. 2009). Finally, TP53 stimulates transcription of the mitochondrial glutaminase GLS2, leading to increased mitochondrial respiration rate and reduced ROS levels (Hu et al. 2010).

The great majority of tumor cells generate energy through aerobic glycolysis, rather than the much more efficient aerobic mitochondrial respiration, and this metabolic change is known as the Warburg effect (Warburg 1956). Since the majority of tumor cells have impaired TP53 function, and TP53 regulates a number of genes involved in glycolysis and mitochondrial respiration, it is likely that TP53 inactivation plays an important role in the metabolic derangement of cancer cells such as the Warburg effect and the concomitant increased tumorigenicity (reviewed by Feng and Levine 2010). On the other hand, some mutations of TP53 in Li-Fraumeni syndrome may result in the retention of its wild-type metabolic activities while losing cell cycle and apoptosis functions (Wang et al. 2013). Consistent with such human data, some mutations of p53, unlike p53 null state, retain the ability to regulate energy metabolism while being inactive in regulating its classic gene targets involved in cell cycle, apoptosis and senescence. Retention of metabolic and antioxidant functions of p53 protects p53 mutant mice from early onset tumorigenesis (Li et al. 2012).

Identifier: R-HSA-5339716
Species: Homo sapiens
Compartment: cytosol
GSK3beta is subject to in-frame missplicing in CML stem cells resulting in the production of mutant protein that lacks the AXIN and FRAT binding domains. Cells containing this mutant GSK3beta show elevated levels of nuclear beta-catenin and enhanced TCF-dependent reporter activity (Jamieson et al, 2008; Abrahamsson et al, 2009).
Identifier: R-HSA-9703465
Species: Homo sapiens
Compartment: cytosol
In addition to internal tandem duplications and activating point mutations, FLT3 is also subject at low frequency to translocations that generate fusion proteins. These fusion proteins occur in some chronic myeloid leukemias as well as myeloid neoplasms with eosinophilia, and generate constitutively active proteins by virtue of fusing a N-terminal partner encoding a dimerization domain with the intracellular region of FLT3 (reviewed in Reiter and Gotlib, 2017; Kazi and Roonstrand, 2019). To date, 6 fusion partner genes of FLT3 have been identified: ETV6, TRIP11, MYO18A, SPTBN1, GOLGB1 and ZMYM2 (Balwin et al, 2007; Vu et al, 2006; Walz et al, 2011; Falchi et al, 2014; Chung et al, 2017; Troadec et al, 2017; Grand et al, 2007; Jawhar et al, 2017; Zhang et al, 2018).
Identifier: R-HSA-1169408
Species: Homo sapiens
Compartment: cytosol
Interferon-stimulated gene 15 (ISG15) is a member of the ubiquitin-like (Ubl) family. It is strongly induced upon exposure to type I Interferons (IFNs), viruses, bacterial LPS, and other stresses. Once released the mature ISG15 conjugates with an array of target proteins, a process termed ISGylation. ISGylation utilizes a mechanism similar to ubiquitination, requiring a three-step enzymatic cascade. UBE1L is the ISG15 E1 activating enzyme which specifically activates ISG15 at the expense of ATP. ISG15 is then transfered from E1 to the E2 conjugating enzyme UBCH8 and then to the target protein with the aid of an ISG15 E3 ligase, such as HERC5 and EFP. Hundreds of target proteins for ISGylation have been identified. Several proteins that are part of antiviral signaling pathways, such as RIG-I, MDA5, Mx1, PKR, filamin B, STAT1, IRF3 and JAK1, have been identified as targets for ISGylation. ISG15 also conjugates some viral proteins, inhibiting viral budding and release. ISGylation appears to act either by disrupting the activity of a target protein and/or by altering its localization within the cell.
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