Search results for STAT1

Showing 20 results out of 280

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Protein (4 results from a total of 18)

Identifier: R-HSA-909686
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: STAT1: P42224
Identifier: R-HSA-909676
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: STAT1: P42224
Identifier: R-HSA-3132766
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: STAT1: P42224
Identifier: R-HSA-6788624
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: STAT1: P42224

Set (4 results from a total of 27)

Identifier: R-HSA-9010176
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-6788573
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-1112574
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-9757476
Species: Homo sapiens
Compartment: cytosol

Reaction (4 results from a total of 139)

Identifier: R-HSA-9851142
Species: Homo sapiens
Compartment: cytosol
STAT1 and STAT3 are phosphorylated in ALK+ and ALK- ALCL in a manner that depends on active TYK2. Knockout or inhibition of TYK2 in ALCL human and mouse models abrogates STAT1 and STAT3 phosphorylation, decreases expression of MCL1 and increases cell death, implicating a TYK2-STAT-MCL signaling cascade in ALCL cell survival (Prutsch et al, 2019). Direct phosphorylation of STAT1 and STAT3 by TYK2 has not been demonstrated, nor has direct binding of either STAT to the promoter of the MCL1 gene, despite previous evidence supporting a JAK/STAT/MCL1 pathway (Prutsch et al, 2019; Rassidakis et al, 2002). Moreover, although autocrine stimulation of IL10 and IL22 has been implicated in the activation of TYK2 in these cells, the precise mechanism for TYK2 upregulation in ALCLs has not been determined (Prutsch et al, 2019).
STAT3 is a known effector of NPM1-ALK-mediated signaling, but the role of STAT1 is somewhat less clear (Crescenzo et al, 2015; Chiarle et al, 2005; reviewed in Chiarle, 2008). STAT1 has been described as a tumor suppressor in ALCL, and one study showed that STAT1 is downregulated in ALCL in an NPM1-ALK- and proteasome-dependent fashion (Wu et al, 2015; Avalle et al, 2012; Zhang and Liu, 2017).
Identifier: R-HSA-1888198
Species: Homo sapiens
Compartment: cytosol
Expression of FGFR1OP-FGFR1 in both Ba/F3 and Cos-1 cells leads to phosphorylation of STAT1 and STAT3 but not STAT5, and to activation of a STAT1/3-responsive reporter when expressed in NIH3T3 cells (Guasch, 2001). Activation of STAT proteins has also been shown to be oncogenic in the context of derivatives of FGFR1, 3 and 4 that lack the extracellular domain and are are targetted to the plasma membrane by a myristylation signal (Hart et al, 2000).
Identifier: R-HSA-8987150
Species: Homo sapiens
Compartment: cytosol, extracellular region, plasma membrane
Signal transducer and activator of transcription 1 alpha/beta (STAT1) and Signal transducer and activator of transcription 3 (STAT3) are believed to be phosphorylated after binding the Interleukin-24 (IL24) receptor complex (Parrish Novak et al. 1998, Andoh et al. 2009, Wang et al. 2002). This complex consists of IL24 ligand, phosphorylated Interleukin-20 receptor subunit alpha (IL20RA), phosphorylated Tyrosine-protein kinase JAK1 (JAK1), Interleukin-20 receptor subunit beta (IL20RB) and STAT1 or STAT3 .
This is a black box event because STAT binding is inferred to precede STAT phosphorylation.
Identifier: R-HSA-9021334
Species: Homo sapiens
Compartment: nucleoplasm
STAT1 can bind to STAT response elements in the HEY1 gene promoter and enhances HEY1 transcription induced by NICD3 (Boelens et al. 2014).

Complex (4 results from a total of 73)

Identifier: R-HSA-8985925
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-873824
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-877297
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-997303
Species: Homo sapiens
Compartment: cytosol

Pathway (4 results from a total of 19)

Identifier: R-HSA-450282
Species: Homo sapiens
MAPKs are protein kinases that, once activated, phosphorylate their specific cytosolic or nuclear substrates at serine and/or threonine residues. Such phosphorylation events can either positively or negatively regulate substrate, and thus entire signaling cascade activity.

The major cytosolic target of activated ERKs are RSKs (90 kDa Ribosomal protein S6 Kinase). Active RSKs translocates to the nucleus and phosphorylates such factors as c-Fos(on Ser362), SRF (Serum Response Factor) at Ser103, and CREB (Cyclic AMP Response Element-Binding protein) at Ser133. In the nucleus activated ERKs phosphorylate many other targets such as MSKs (Mitogen- and Stress-activated protein kinases), MNK (MAP interacting kinase) and Elk1 (on Serine383 and Serine389). ERK can directly phosphorylate CREB and also AP-1 components c-Jun and c-Fos. Another important target of ERK is NF-KappaB. Recent studies reveals that nuclear pore proteins are direct substrates for ERK (Kosako H et al, 2009). Other ERK nuclear targets include c-Myc, HSF1 (Heat-Shock Factor-1), STAT1/3 (Signal Transducer and Activator of Transcription-1/3), and many more transcription factors.

Activated p38 MAPK is able to phosphorylate a variety of substrates, including transcription factors STAT1, p53, ATF2 (Activating transcription factor 2), MEF2 (Myocyte enhancer factor-2), protein kinases MSK1, MNK, MAPKAPK2/3, death/survival molecules (Bcl2, caspases), and cell cycle control factors (cyclin D1).

JNK, once activated, phosphorylates a range of nuclear substrates, including transcription factors Jun, ATF, Elk1, p53, STAT1/3 and many other factors. JNK has also been shown to directly phosphorylate many nuclear hormone receptors. For example, peroxisome proliferator-activated receptor 1 (PPAR-1) and retinoic acid receptors RXR and RAR are substrates for JNK. Other JNK targets are heterogeneous nuclear ribonucleoprotein K (hnRNP-K) and the Pol I-specific transcription factor TIF-IA, which regulates ribosome synthesis. Other adaptor and scaffold proteins have also been characterized as nonnuclear substrates of JNK.

Identifier: R-HSA-9705462
Species: Homo sapiens
Signaling by CSF3 causes its own inactivation, thereby preventing overproliferation of neutrophils (reviewed in Beekman and Touw 2010, Palande et al. 2013). Activated CSF3R recruits and activates JAK2, which phosphorylates STAT1, STAT3, and STAT5. The phosphorylated STATs transit to the nucleus and enhance the expression of SOCS1 and SOCS3, inhibitors of CSF3R signaling (inferred from mouse homologs). SOCS3, the principle negative regulator, binds the phosphorylated C-terminal region of CSF3R (Hörtner et al. 2002, van de Geijn et al. 2004, and inferred from mouse homologs) and acts in two ways: direct inhibition of the phosphorylation activity of JAK2 (van de Geijn et al. 2004) and promotion of endocytosis (Ward et al. 1999, Aarts et al. 2004, Irandoust et al. 2007) and ubiquitination (Irandoust et al. 2007, Wölfler et al. 2009) of CSF3R.
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.
Identifier: R-HSA-877300
Species: Homo sapiens
Interferon-gamma (IFN-gamma) belongs to the type II interferon family and is secreted by activated immune cells-primarily T and NK cells, but also B-cells and APC. INFG exerts its effect on cells by interacting with the specific IFN-gamma receptor (IFNGR). IFNGR consists of two chains, namely IFNGR1 (also known as the IFNGR alpha chain) and IFNGR2 (also known as the IFNGR beta chain). IFNGR1 is the ligand binding receptor and is required but not sufficient for signal transduction, whereas IFNGR2 do not bind IFNG independently but mainly plays a role in IFNG signaling and is generally the limiting factor in IFNG responsiveness. Both IFNGR chains lack intrinsic kinase/phosphatase activity and thus rely on other signaling proteins like Janus-activated kinase 1 (JAK1), JAK2 and Signal transducer and activator of transcription 1 (STAT-1) for signal transduction. IFNGR complex in its resting state is a preformed tetramer and upon IFNG association undergoes a conformational change. This conformational change induces the phosphorylation and activation of JAK1, JAK2, and STAT1 which in turn induces genes containing the gamma-interferon activation sequence (GAS) in the promoter.
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