Dual specificity tyrosine-phosphorylation-regulated kinase 1A is an enzyme that in humans is encoded by the DYRK1A gene. (wikipedia.org)
DYRK1A is a member of the dual-specificity tyrosine phosphorylation-regulated kinase (DYRK) family. (wikipedia.org)
Homeodomain-interacting protein kinases (HIPKs) belong to the CMGC kinase family and are closely related to dual-specificity tyrosine phosphorylation-regulated kinases (DYRKs). (nature.com)
HIPKs belong to the CMGC group of serine/threonine kinases and are part of the dual-specificity tyrosine phosphorylation-regulated kinase (DYRK) family. (nature.com)
Brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4) activated the FL receptor, as determined by tyrosinephosphorylation. (jneurosci.org)
Binding of Sema4D to plexin-B1 stimulates the intrinsic tyrosine kinase activity of ErbB-2, resulting in the phosphorylation of both plexin-B1 and ErbB-2. (rupress.org)
It can inhibit the phosphorylation reaction through competing with adenosine triphosphate to bind to the catalytic region of the receptor tyrosine kinase, thereby blocking the down-proliferation signaling and inhibiting the activity of the tumor cell ligand-dependent HER-1/EGFR, thus achieving the inhibition of the proliferation of tumor cells. (lookchem.com)
Phosphorylation of EGFR at certain residues is also mediated by Src-non-receptor kinase. (thermofisher.com)
BTK, a TEC-family tyrosine kinase activated by the B-cell antigen receptor, contains a variety of regulatory domains and it is subject to complex regulation by membrane phospholipids, protein ligands, phosphorylation, and dimerization. (elifesciences.org)
The binding of extracellular matrix ligands to integrins triggers autophosphorylation at Tyr-397, and activation of FAK through phosphorylation of Tyr residues (Tyr-576 and Tyr577) in the kinase domain activation loop. (fishersci.com)
In addition, phosphorylation of other Tyr residues (Tyr-925, and Tyr-861) creates binding sites for SH2 domains of intracellular signaling molecules such as Src, PI3 kinase, and Grb2. (fishersci.com)
Phosphorylation at Tyr-568 is required for interaction with PTPN11/SHP-2, CRK (isoform Crk-II) and members of the SRC tyrosine-protein kinase family. (arigobio.com)
Here, using baculoviral co-expression of the DDR2 cytosolic domain and Src, we show that Src targets three tyrosine residues (Tyr-736, Tyr-740, and Tyr-741) in the activation loop of DDR2 for phosphorylation. (korea.ac.kr)
Phosphorylation of receptor serine/threonine residues has been proposed to exert an inhibitory influence on receptor tyrosine kinase activity and Ser 1327 and Thr 1348 have been identified as specific sites of phosphorylation in the insulin receptor COOH terminal domain. (jci.org)
To address the potential negative regulatory role of phosphorylation of these residues in vivo, we assessed the extent of phosphorylation of each site in insulin receptor isolated from the skeletal muscle of 12 NIDDM patients and 13 nondiabetic, control subjects. (jci.org)
Moreover, within each group there was no correlation between the level of tyrosine kinase activity and the extent of serine/threonine phosphorylation. (jci.org)
It is concluded that the stoichiometry of serine/threonine phosphorylation of insulin receptor in vivo is low, and that increased phosphorylation of Ser 1327 or Thr 1348 is not responsible for the decreased insulin receptor tyrosine kinase activity observed in the skeletal muscle of NIDDM patients. (jci.org)
Tyrosine phosphorylation initiates multiple signaling pathways including RAS, PI3 kinase, Src, and JAK/STAT. However, SCF is a versatile factor in the differentiation of many specific cell types like spermatogonial stem cells and megakaryocyte progenitors. (biofargo.com)
Violin plots show distribution of expression levels for Dual specificity tyrosine-phosphorylation-regulated kinase 2 (SMED30002728) in cells (dots) of each of the 12 neoblast clusters. (stowers.org)
Expression of Dual specificity tyrosine-phosphorylation-regulated kinase 2 (SMED30002728) in the t-SNE clustered sub-lethally irradiated X1 and X2 cells. (stowers.org)
Violin plots show distribution of expression levels for Dual specificity tyrosine-phosphorylation-regulated kinase 2 (SMED30002728) in cells (dots) of each of the 10 clusters of sub-leathally irradiated X1 and X2 cells. (stowers.org)
Epidermal growth factor receptor (EGF R, also known as ErbB1 and HER1) is the founding member of the ErbB family of receptor tyrosine kinases. (rndsystems.com)
The trk receptors, a family of receptor tyrosine kinases including trkA, trkB, and trkC, serve as the principal signal-transducing receptors for the neurotrophins ( Barbacid, 1994 ). (jneurosci.org)
EGFR belongs to the HER/ERbB family of proteins that includes three other receptor tyrosine kinases, ERbB2, ERbB3, ERbB4. (thermofisher.com)
The TEC kinases are the second largest sub-family of non-receptor tyrosine kinases in the human genome after the SRC family [ 1 - 3 ]. (elifesciences.org)
NTRK receptors, NTRK1 (TRKA), NTRK2 (TRKB) and NTRK3 (TRKC) are receptor tyrosine kinases activated by ligand binding to their extracellular domain. (reactome.org)
The ErbB family consists of four plasma membrane-bound receptor tyrosine kinases. (iiab.me)
FGF activity is mediated by a family of type I transmembrane tyrosine kinases, which undergo dimerization and autophosphorylation after ligand binding. (rndsystems.com)
The ligand-bound TM configuration promotes asymmetric dimerization of the intracellular juxta-membrane (JM) and kinase domains, which causes autophosphorylation of intracellular tyrosine residues ( 6 , 7 ). (biorxiv.org)
EGFR is a transmembrane receptor and binding of its cognate ligands such as EGF (Epidermal Growth Factor) and TGF alpha (Transforming Growth Factor alpha) to the extracellular domain leads to EGFR dimerization followed by autophosphorylation of the tyrosine residues in the cytoplasmic domain. (thermofisher.com)
Membrane-induced dimerization activates BTK and we present here a crystal structure of an activation loop swapped BTK kinase domain dimer that likely represents the conformational state leading to trans-autophosphorylation. (elifesciences.org)
Ligand binding induces receptor dimerization, followed by trans-autophosphorylation of dimerized receptors on conserved tyrosine residues in the cytoplasmic region. (reactome.org)
Binding of SCF to C-kit induces receptor dimerization and autophosphorylation of tyrosine residues in the cytoplasmic domain. (biofargo.com)
Cytoplasmic domain2
For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. (arigobio.cn)
Dimerisation results in the autophosphorylation of tyrosine residues within the cytoplasmic domain of the receptors and initiates a variety of signaling pathways. (iiab.me)
EGFR4
Gefitinib administration prevents tyrosine residue of autophosphorylation of the EGFR receptor. (pharmacology2000.com)
The small molecule compound, Erlotinib is a receptor tyrosine kinase inhibitor (EGFR antagonist) and belongs to molecular targeted therapy Drugs. (lookchem.com)
Ligand5
The PDGFRβ is heavily phosphorylated on numerous tyrosine residues through both autophosphorylation and ligand-dependent processes. (biolegend.com)
Because positively charged residues in NT-3 are important for binding to trkB, two negatively charged aspartate residues within the 11 amino acid motif of FL trkB were mutated to examine the role of electrostatic interactions on ligand binding. (jneurosci.org)
Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. (joplink.net)
They signal through two types of receptors: NTRK (TRK) tyrosine kinase receptors (TRKA, TRKB, TRKC), which differ in their preferred neurotrophin ligand, and p75NTR death receptor, which interacts with all neurotrophins. (reactome.org)
Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. (arigobio.cn)
Proteins4
Phosphorylated tyrosines in the intracellular domain of the receptor serve as docking sites for adapter proteins, triggering downstream signaling cascades. (reactome.org)
Signaling proteins are recruited to activated c-Kit by certain interaction domains that specifically bind to phosphorylated tyrosine residues in the intracellular region of c-Kit. (biofargo.com)
Upon cytokine activation receptor chain- bound STATs are then phosphorylated on the tyrosine residues, which results in dimerisation of STAT proteins that translocate to the nucleus and activate gene transcription. (openrheumatologyjournal.com)
1 Insulin receptor functions as an enzyme that transfers phosphate groups from ATP to tyrosine residues on intracellular target proteins. (sputnic-group.ru)
Induces1
IGF-1R induces activation and autophosphorylation of particular tyrosine kinase residues, initiating signaling cascades such as for example Ras/Raf/mitogen-activated protein kinases (MAPK) and phosphoinositide 3-kinase (PI3K), that are oncoproteins involved with many cellular activities [13] downstream. (2011globalhealth.org)
These findings suggest that tyrosine 740 inhibits DDR2 autophosphorylation. (korea.ac.kr)
Insulin5
The tyrosine kinase activity of insulin receptor isolated from the skeletal muscle of NIDDM patients has previously been found to be decreased compared with the activity of receptor from nondiabetic subjects but the mechanism underlying this defect is unknown. (jci.org)
The extent of insulin-induced tyrosine autophosphorylation was decreased in receptor isolated from diabetic versus nondiabetic muscle, thus confirming earlier reports. (jci.org)
The insulin receptor is a receptor tyrosine kinase (RTK) that conformationally consists of two alpha and two beta subunit tetramers. (encyclopedia.pub)
The insulin receptor exhibiting kinase activity is responsible for its autophosphorylation at the tyrosine residue site upon insulin binding. (encyclopedia.pub)
Binding of insulin to the alpha subunits causes the beta subunits to phosphorylate themselves (autophosphorylation), thus activating the catalytic activity of the receptor. (sputnic-group.ru)
Kinase domains1
The family is defined by structural similarity of their kinase domains and their capability to autophosphorylate on tyrosine residues. (antibodies-online.com)
Ligands2
Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. (joplink.net)
Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. (arigobio.com)
This gene product is a protein tyrosine kinase involved in a specific subset of cytokine receptor signaling pathways. (arigobio.cn)
Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. (drugbank.com)
Receptor tyrosine-protein kinase erbB-2 , also known as CD340 (cluster of differentiation 340), proto-oncogene Neu , Erbb2 (rodent), or ERBB2 (human), is a protein that in humans is encoded by the ERBB2 gene. (iiab.me)
ErbB1
Here, we show that plexin-B family members stably associate with the receptor tyrosine kinase ErbB-2. (rupress.org)
ALK , the chromosome 2 gene locus altered by the t(2;5) in non-Hodgkin's lymphoma, encodes a novel neural receptor tyrosine kinase that is highly related to leukocyte tyrosine kinase (LTK). (nature.com)
Phosphorylate1
DYRKs are named after their characteristic dual-specificity, as they auto-phosphorylate a conserved tyrosine in their activation loop, but phosphorylate substrates on serine and threonine residues 2 . (nature.com)
Molecular weight1
CD140b contains two immunoglobulin-like domains and a tyrosine kinase domain with a predicted molecular weight approximately 124 kD. (biolegend.com)
Domain3
Linker regions and domains are labeled, residue numbering shows BTK domain boundaries. (elifesciences.org)
In vitro She binding assays demonstrate that phosphotyrosines resulting from DDR2 autophosphorylation are involved in Shc binding to the DDR2 cytosolic domain. (korea.ac.kr)
3) DDR2 autophosphorylation generates cytosolic domain phosphotyrosines that promote the formation of DDR2 cytosolic domain-Shc signaling complexes. (korea.ac.kr)
DYRK1
For the class II DYRK ortholog from D. melanogaster it was demonstrated that the critical tyrosine is cis -auto-phosphorylated by the nascent kinase in a transitory intermediate state during maturation at the ribosome 3 . (nature.com)
Signaling2
Roles for Eph receptor tyrosine kinase signaling in the formation of topographic patterns of axonal connectivity have been well established in vertebrate visual systems. (sdbonline.org)
Phosphorylated on tyrosine residues in response to interferon gamma signaling (PubMed:7615558, PubMed:7673114). (arigobio.cn)
Exert1
Latest studies exposed that obstructing IGF-1R pathway, such as for example little molecule tyrosine kinase inhibitor (TKI, linsitinib) and monoclonal antibodies, can exert appealing effects for the treating numerous kinds of tumor in medical trials [23]. (2011globalhealth.org)
Autophosphorylation on Tyr-119 in response to EPO down-regulates its kinase activity (By similarity). (arigobio.cn)
Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972 in response to growth hormone (GH) are required for maximal kinase activity (By similarity). (arigobio.cn)
The TEC family kinase, BTK (Bruton's tyrosine kinase) is best known as the target of ibrutinib (IMBRUVICA®), the first-in-class covalent kinase active site inhibitor used to treat chronic lymphocytic leukemia (CLL), mantle cell lymphoma (MCL), Waldenström's macroglobulinemia (WM), and chronic graft-versus-host disease (cGVHD). (elifesciences.org)
Processes1
Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. (arigobio.cn)
Domains1
FGFRs contain three Ig-like domains and a stretch of acidic residues between the first and second Ig-like domains. (rndsystems.com)
Genes1
To better understand the molecular changes associated with AD, genome-wide association studies (GWAS) have identified hundreds of candidate genes linked to the disease, like the receptor tyrosine kinase EphA1. (sdbonline.org)
Interaction1
Finally, the C-terminus of HIPK1-3 comprises a region rich in serine, glutamine, and alanine (SQA) residues, which is involved in the interaction with different co-factors 14 . (nature.com)
Human1
Hallberg, B. & Palmer, R. H. Mechanistic insight into ALK receptor tyrosine kinase in human cancer biology. (nature.com)
Role1
A role for a Drosophila Eph receptor tyrosine kinase (Eph) in the control of photoreceptor axon and cortical axon topography in the developing visual system is described. (sdbonline.org)