Threonine protein kinases tyrosine residue phosphorylation of serine residues. Medical search. Frequent questions

AKT/PI3K forms a key component of many signalling pathways that involve the binding of membrane-bound ligands such as receptor tyrosine kinases, G-protein coupled receptors, and integrin-linked kinase. (senescence.info)
Glycogen synthase kinase 3 (GSK-3) / SHAGGY kinase (SGG) are multifunctional non receptor serine/threonine kinases. (biomedcentral.com)
instead cytokines function through binding to a cognate receptor proteins, which trigger phosphorylation and activation of intracellular signaling proteins. (openrheumatologyjournal.com)
The binding of a growth factor brings the multiple monomeric receptor chains into close proximity resulting into the trans-phosphorylation of their cytoplamic domains, which consequently activates downstream signaling cascades. (openrheumatologyjournal.com)
Formation of the cytokine receptor / JAK signaling complex and activation of JAK kinases leads to the phosphorylation of receptor chains, which creates docking sites for STAT ( S ignal T ransducers and A ctivators of T ranscription) transcription factors. (openrheumatologyjournal.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)
Normally, upon the stimulations by growth factors (GFs), the receptor tyrosine kinases (RTKs) are activated, and then recruit PI3K protein complex on the membrane to generate phosphatidylinositol-3,4,5-triphosphate (PIP3) from phosphatidylinositol-4,5-biophosphate (PIP2) [ 2 ]. (biomedcentral.com)
Receptor Tyrosine Kinases (RTKs) are a family of tyrosine protein kinases. (callaix.com)
Imatinib, for example, blocks a kinase receptor from binding to ATP, preventing the phosphorylation that would benefit the cancerous cell and promote cell division. (callaix.com)

Protease and phosphatase inhibitors are essential components of most cell lysis and protein extraction procedures. (thermofisher.com)
In whole cells, protease and phosphatase activities are tightly regulated by compartmentalization or inhibitors to prevent indiscriminate damage to cellular proteins and to maintain proper function of signaling pathways. (thermofisher.com)
Protease and phosphatase inhibitors can be added to the lysis reagents in order to prevent degradation of extracted proteins, and to obtain the best possible protein yield and activity following cell lysis. (thermofisher.com)
Proteases inhibitors are nearly always needed, while phosphatase inhibitors are required only when phosphorylation states (activation states) are being investigated. (thermofisher.com)
STP, serine/threonine protein phosphatase. (rupress.org)
PIP3 phosphatase PTEN is inactivated upon phosphorylation in its C-terminal region by several serine/threonine kinases [ 12 ]. (biomedcentral.com)
Bien que considérée dans le passé comme une enzyme constitutive non spécifique, PP2A est une phosphatase soumise à une régulation précise et qui est importante dans le contrôle des fonctions cellulaires impliquant la phosphorylation. (ac.be)
Although intracellular signal transduction is often portrayed as a protein kinase 'domino effect', the counterbalancing function of phosphatases, and thus the control of phosphatase activity, is equally relevant to proper regulation of cellular function. (ac.be)
Protein Phosphatase 2A (PP2A) is a widely expressed family of protein phosphatases made of a core dimer, composed of a catalytic (C) subunit and a structural (A) subunit, in association with a third variable regulatory (B) subunit. (ac.be)
Although viewed as a constitutive housekeeping enzyme in the past, PP2A is a highly regulated phosphatase and is emerging as an important regulator of multiple cellular processes involving protein phosphorylation. (ac.be)
2 Protein phosphatase 2A (PP2A) is a very abundant - it accounts for as much as 1% of total cellular proteins - ubiquitous and remarkably conserved enzyme. (ac.be)
Activation loop phosphorylations of Akt1, PKA and PKC take place at threonine 308, threonine 197 and threonine 403, respectively (Fig. 1B).6,7 Open up in another window Body 1 Evaluation of ATP-regulated phosphatase resistant set ups of AGC kinases. (pkc-inhibitor.com)
It is well understood that changes in phosphorylation signaling can be due to deregulation of kinase and phosphatase function, usually detected through altered gene expression. (ubigene.us)
Amino acid substitutions on kinases or phosphatases directly interrupt the stability and/or the function of the kinase or phosphatase, resulting in changes in target phosphorylation. (ubigene.us)
Effects of kinase or phosphatase regulators can also lead to altered phosphorylation. (ubigene.us)

In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. (embl.de)
One of these events is protein phosphorylation, which when altered may result in system-wide disruption and deregulation of signal transduction. (ubigene.us)
A mechanism of signal transduction deregulation in cancer is mediated by either removal or creation of phosphorylation sites thereby causing either a loss or a gain of phosphorylation function, depending on the role of the phosphorylated residue. (ubigene.us)

However, it is recognised that for many protein kinase families, particularly those that phosphorylate Ser/Thr residues, peptide specificity is the major factor that determines substrate specificity. (biomedcentral.com)
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)

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)
Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. (rcsb.org)
It does not include the catalytic domain of dual specificity kinases. (rcsb.org)

Fibroblast growth factor 1 (FGF1) acts by activating specific tyrosine kinase receptors on the cell surface. (bvsalud.org)
Growth factor cytokine receptors typically have intrinsic kinase activity. (openrheumatologyjournal.com)
In contrast, classical immune (type I/ II) cytokine receptors do not have intrinsic protein kinase activity but associate with the Janus family of kinases (JAKs). (openrheumatologyjournal.com)

In vitro kinase assays showed that TaSK1 and TaSK2 possessed kinase activity. (biomedcentral.com)
In vitro kinase assay is applied to identify the kinase of PIK3CA/p110α tyrosine phosphorylation. (biomedcentral.com)

intracellular degrees of cyclic AMP and cyclic GMP activate proteins kinase 163222-33-1 A (PKA) and proteins kinase G (PKG), respectively. (pkc-inhibitor.com)

The reversible phosphorylation of proteins on serine, threonine, and tyrosine residues represents a fundamental strategy used by eukaryotic organisms to regulate a host of biological functions, including DNA replication, cell cycle progression, energy metabolism, and cell growth and differentiation. (rupress.org)

These inhibitors block or inactivate endogenous proteolytic and phospholytic enzymes that are released from subcellular compartments during cell lysis and would otherwise degrade proteins of interest and their activation states. (thermofisher.com)
Research experiments may necessitate the use of single inhibitors or customized mixtures, but most protein work is best served by using a suitable protease inhibitor cocktail . (thermofisher.com)
Also provided are methods of treatment as Janus Kinase inhibitors and pharmaceutical compositions containing the compounds of the invention and combinations thereof with other therapeutic agents. (justia.com)
In the next step, FGF1 variants with mutated or deleted NLS were expressed in U2OS cells, in which apoptosis was then induced by various factors (e.g., starvation, etoposide, staurosporine, anisomycin and actinomycin D). Experiments were performed in the presence of specific FGFR inhibitors to eliminate FGFR-induced signaling, potentially activated by FGF1 proteins released from damaged cells. (bvsalud.org)
Kinase inhibitors are now one of the major categories of chemotherapy medicine. (callaix.com)
Over 50 kinase inhibitors are approved in the US for cancer treatment with more under development. (callaix.com)
Of the 69 new drugs approved by the FDA for cancer from 2015 to 2020, 26 were kinase inhibitors. (callaix.com)
Most kinase inhibitors work on tyrosine kinases . (callaix.com)
As oncology drugs, kinase inhibitors were created out of modern genetics- the understanding of DNA, the cell cycle, and molecular signaling pathways- and thus represent a change from general to molecular methods of cancer treatment. (callaix.com)
An article published in the journal Molecular Cancer in 2018 claimed that over 10,000 patents had been filed in the US for kinase inhibitors since 2001. (callaix.com)
Tyrosine kinase inhibitors (TKIs) are a class of chemotherapy medications that inhibit, or block, one or more of the enzyme tyrosine kinases. (callaix.com)
Tyrosine kinase inhibitors treat cancer by correcting this deregulation. (callaix.com)

Either at genomic or at proteomic level, mutations have significant impact on normal gene or protein function, and human diseases could be associated with mutations like nonsynonymous single-nucleotide variations (nsSNVs) on amino acids. (hindawi.com)
Protein enzymes are chains of amino acids and when a phosphoryl group, PO32−, is covalently attached to one of the amino acids, it changes the three-dimensional configuration and function of the protein. (callaix.com)
4 While proteins can be phosphorylated on nine amino acids, serine, threonine and tyrosine phosphorylation are by far the most predominant in eukaryotic cells. (ac.be)
In another study in catenin β-1, which is involved in hepatocarcinoma, phosphorylation is known to occur on amino acids T41 and S45 and result in significant scores for loss-of-phosphorylation. (ubigene.us)

methylation at certain residues of histones can regulate gene expression [ 4 ], and glycosylation is responsible for targeting substrates and changing protein half-life [ 2 ]. (hindawi.com)
Protein kinases and their substrates regulate essentially all cellular processes through complex regulatory networks, in which phosphorylated proteins act as switches that tune the response of the cell to environmental stimuli. (biomedcentral.com)
Protein phosphorylation can regulate enzyme function, mediate protein-protein interactions, alter subcellular localization, and control protein stability. (rupress.org)
These AKT proteins therefore regulate a wide variety of cellular functions including cell proliferation, survival, metabolism, and angiogenesis in both normal and malignant cells. (senescence.info)
p110s perform lipid kinase activity, and p85s stabilize and regulate p110s. (biomedcentral.com)
Akt Kinase Allosteric Conformations Regulate Akt Activation Loop Phosphorylation The majority of this prior work centered on molecular systems managing kinase activation. (pkc-inhibitor.com)

We have previously described an approach to predicting the substrate specificity of serine-threonine protein kinases. (biomedcentral.com)
The relative contribution of substrate recruitment and peptide specificity to protein kinase substrate specificity varies between protein kinases. (biomedcentral.com)

To this end, we produced recombinant FGF1 variants with mutated or deleted NLS and added them to apoptosis-induced cells in which FGFR1 was inactive, either as a result of chemical inhibition or kinase-dead mutation. (bvsalud.org)
Scientists are looking the possibility of kinase inhibition for other diseases including hypertension and Parkinson's disease but here we focus on cancer medicines. (callaix.com)

another is mutation of T286 in cyclin D1 (CCND1) causing the loss of phosphorylation of T286 is involved in nuclear accumulation of cyclin D1 in esophageal cancer [ 14 ]. (hindawi.com)
Phosphorylation of T286 by GSK3B in the wild type form of cyclin D1 initiates its nuclear export and subsequent degradation in the cytoplasm, while the loss of phosphorylation is causatively implicated in nuclear accumulation of cyclin D1 in esophageal cancer and generally increased oncogenic potential. (ubigene.us)
Notably, the Wnt/β-Catenin pathway is enriched in both the gain and loss of phosphorylation sites. (ubigene.us)

Predikin now consists of two components: (i) PredikinDB, a database of phosphorylation sites that links substrates to kinase sequences and (ii) a Perl module, which provides methods to classify protein kinases, reliably identify substrate-determining residues, generate scoring matrices and score putative phosphorylation sites in query sequences. (biomedcentral.com)
The new features significantly enhance the ability of Predikin to analyse protein kinases and their substrates. (biomedcentral.com)
In general, a protein kinase acts on a discrete set of substrates to ensure that signalling fidelity is maintained. (biomedcentral.com)
The prediction of peptide specificity is therefore the basis for most of the available computational methods aimed at predicting substrates of protein kinases. (biomedcentral.com)

Known phosphatases are specific for cleavage of either serine-threonine or tyrosine phosphate groups. (thermofisher.com)
Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. (rcsb.org)
These enzymes promote transfer of a gamma phosphate group from ATP to a tyrosine residue on a protein. (callaix.com)
The removal of a phosphate group changes the shape and actions of the protein. (callaix.com)
When the cellular action(s) is completed, the phosphate group is removed and that protein is "turned off. (callaix.com)
PKA, PKB, PKC Intro Protein kinases improve proteins function 163222-33-1 by attaching phosphate organizations to specific proteins. (pkc-inhibitor.com)

Many of the cellular proteins are kept separate from proteolytic enzymes. (thermofisher.com)
Protein kinases, the enzymes responsible for protein phosphorylation, make up almost 2% of protein-encoding genes in the human genome [ 1 ] and an estimated 30-50% of human proteins are phosphorylated [ 2 ]. (biomedcentral.com)
Protein kinases are families of enzymes that catalyze the phosphorylation of specific residues in proteins, broadly classified into tyrosine and serine/threonine kinases. (justia.com)
Thus, protein kinases have emerged as an important class of enzymes as targets for therapeutic intervention. (justia.com)
In the past, most of the attention was focused primarily on protein kinases and on their regulation, mainly because phosphatases were then viewed as simple housekeeping enzymes. (ac.be)
But advances in the understanding of protein phosphatases make now clear that these enzymes are precisely regulated and are as important as kinases in the regulation of cellular processes involving protein phosphorylation. (ac.be)

Tyrosine phosphorylation of RTKs, or adaptor proteins such as IRS-1 facilitate their binding with p85 regulatory subunits of PI3K, and then bring PI3K complex on membrane [ 2 ]. (biomedcentral.com)

Disruptions of phosphorylation sites are associated with cancer, for instance, mutations of T286 in cyclin D1 (CCND1). (ubigene.us)

Through extensive biochemical and genetic analysis, we now know that pathways are not simply switched on with kinases and off with phosphatases. (rupress.org)
Phospho-proteomics analysis and Western blots are used to demonstrate downstream signaling pathways of PIK3CA/p110α tyrosine phosphorylation. (biomedcentral.com)
PIK3CA/p110α phosphorylation at Y317 and Y508 play important role in tumorigenesis of colorectal cancer through two independent pathways. (biomedcentral.com)
Phosphorylation disrupting mutations, we can find several pathways are enriched in mutations. (ubigene.us)

Protein degradation during cell lysis. (thermofisher.com)
Disruption of cellular and tissue architecture during protein extraction distorts the in vivo state by making all proteins potentially accessible for degradation or modification by endogenous proteases and phosphatases. (thermofisher.com)
C-terminally adjacent to the HID follows a proline, glutamate, serine, and threonine (PEST)-rich domain, mediating proteasomal degradation of these kinases. (nature.com)

Tyrosine phosphorylation of PIK3CA/p110α is stimulated by growth factors such as EGF, HGF and PDGF. (biomedcentral.com)

The individual kinome of 518 proteins kinases continues to be broadly split into nine useful groups. (pkc-inhibitor.com)

PTMs are involved in many protein activities and cellular processes, such as protein folding, stability, conformation, and some significant regulatory mechanisms [ 1 ]. (hindawi.com)
Crystal structures of protein kinases with bound substrate peptides show that substrate residues at positions -3 to +3 relative to the phosphorylated serine, threonine or tyrosine residue adopt an extended conformation and bind to a pocket in the catalytic domain of the protein kinase [ 8 ]. (biomedcentral.com)
Upon phosphorylation, it goes from the catalytic middle and adopts a conformation which allows ATP and substrate binding, and leads to a shut conformation from the N- and C-lobes. (pkc-inhibitor.com)
B) Structural representation from the secured activation loop conformation in the current presence of ATP in the three AGC kinases. (pkc-inhibitor.com)
Hence, the transition from the inactive Akt kinase towards the energetic conformation needs at least two sequential guidelines impacting the PH area first. (pkc-inhibitor.com)

To fully understand this complex and essential regulatory process, the kinases and phosphatases mediating the changes in cellular phosphorylation must be identified and characterized. (rupress.org)
These highly similar AKT proteins all have an N-terminal pleckstrin homology domain, a serine/threonine-specific kinase domain and a C-terminal regulatory domain. (senescence.info)
1 Reversible protein phosphorylation is an important regulatory mechanism that controls the activities of a myriad of proteins and is thus involved in virtually every major physiological process. (ac.be)

A variety of approaches, including biochemical purification, gene isolation by homology, and genetic screens, have been successfully used for the identification of putative protein kinases and phosphatases. (rupress.org)
The sterile alpha motif (SAM) domain is a putative protein interaction module present in a wide variety of proteins [ ( PUBMED:9007998 ) ] involved in many biological processes. (embl.de)

Kinases are a class of enzyme that promote phosphorylation. (callaix.com)

The method, named Predikin, identifies key conserved substrate-determining residues in the kinase catalytic domain that contact the substrate in the region of the phosphorylation site and so determine the sequence surrounding the phosphorylation site. (biomedcentral.com)
The second factor, termed peptide specificity, describes the interaction between amino acid residues in the catalytic domain of the protein kinase and the substrate residues that surround the phosphorylated residue. (biomedcentral.com)
The heptapeptide sequence from -3 to +3 that best binds to the pocket is determined by the physicochemical nature of the residues in the catalytic domain that line the pocket and contact the substrate. (biomedcentral.com)
This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. (rcsb.org)
AGC kinases, like the 3 Akt (proteins kinase B) isoforms, proteins kinase A (PKA) and everything proteins kinase C (PKC) isoforms, require activation loop phosphorylation (threonine 308 in Akt1) aswell as phosphorylation of the C-terminal residue (serine 473 in Akt1) for catalytic activity and phosphorylation of downstream focuses on. (pkc-inhibitor.com)
Analyses from the X-ray crystallography buildings of PKA supplied vital insights into powerful adjustments in the framework from the kinase area of AGC kinases connected with Ptgfr their activation.2,3 Generally conditions, the catalytic subunits of proteins kinases are defined by two lobes, a smaller sized N-terminal lobe and a more substantial C-terminal lobe (Fig. 1A). (pkc-inhibitor.com)
In lots of kinases, gain access to of ATP and substrate towards the energetic site cleft is certainly controlled with the activation loop, which, by method of phosphorylation, goes through marked conformational adjustments.5 In the unphosphorylated condition, the activation loop is normally disordered and acts to sterically impede gain access to of both nucleotide and substrate towards the catalytic cleft. (pkc-inhibitor.com)

In particular, the JAK family of cellular protein tyrosine kinases (JAK1, JAK2, JAK3, and TYK2) play a central role in cytokine signaling (Kisseleva et al. (justia.com)

The post-translational modification of proteins by phosphorylation of serine, threonine or tyrosine residues is a ubiquitous process in cellular regulation. (biomedcentral.com)

Yet how gene mutations affect protein activities through posttranslational modification sites have not been widely studied. (hindawi.com)

Protein phosphatases act as negative regulators of AKT proteins by dephosphorylating AKT or PIP3. (senescence.info)

Phosphorylation is the most common post-translational modification on proteins, with approximately 80% occurring on serine, 20% on threonine, and 0.1 to 1% on tyrosine residues. (thermofisher.com)

Phosphorylation from the Akt/PKB activation loop is certainly additional constrained by close apposition from the N-terminal pleckstrin homology (PH) area concealing threonine 308.8,9 This constraint is relieved by membrane translocation and binding to PtdIns(3,4,5)P3 lipids which unmask the unphosphorylated activation loop (threonine 308 in Akt1). (pkc-inhibitor.com)

Such compounds are useful for inhibiting Janus Kinases (JAKs). (justia.com)
Janus kinases (Jaks) are critical signaling elements for a large subset of cytokines. (openrheumatologyjournal.com)

Subsequent phosphorylation of both threonine residue 308 and serine residue 473 is required for full activation of the AKT1 protein encoded by this gene. (senescence.info)
Nevertheless, ATP and Mn2+ and matching Akt1 amino acidity residues are indicated for clearness. (pkc-inhibitor.com)

In factor of the need for AGC proteins kinases in regulating cell 163222-33-1 destiny, the molecular systems that control the phosphorylation of the kinases have already been examined thoroughly. (pkc-inhibitor.com)

Rather, a mixture or inhibitor cocktail of several different inhibitor compounds are used to ensure that protein extracts do not degrade before analysis for targets of interest. (thermofisher.com)
M any kinase inhibitor compounds have been found. (callaix.com)

Adding further complexity to this picture is the fact that both kinases and phosphatases can function in signaling networks where multiple kinases and phosphatases contribute to the outcome of a pathway. (rupress.org)
AKT proteins also participate in the mammalian target of rapamycin (mTOR) signalling pathway which controls the assembly of the eukaryotic translation initiation factor 4F (eIF4E) complex and this pathway, in addition to responding to extracellular signals from growth factors and cytokines, is disregulated in many cancers. (senescence.info)
Protein phosphorylation is crucial for signaling transduction of this pathway. (biomedcentral.com)
Post-translational modifications (PTMs) are crucial for regulating PI3K/AKT signaling pathway, notably phosphorylation. (biomedcentral.com)

Protein posttranslational modifications (PTMs) play key roles in a variety of protein activities and cellular processes. (hindawi.com)
Different PTMs show distinct impacts on protein functions, and normal protein activities are consequences of all kinds of PTMs working together. (hindawi.com)
More than 200 different types of protein posttranslational modifications (PTMs) have been detected. (hindawi.com)
More than two-thirds of the 21,000 proteins encoded by the human genome is phosphorylated, and, likely, more than 90% are subjected to PTMs. (ubigene.us)

The FGF1 protein contains a specific N-terminal nuclear localization sequence (NLS) that is essential for its efficient transport to the nucleus. (bvsalud.org)
cSH2 domain S690 phosphorylation decreases p85 binding affinity to tyrosine-phosphorylated proteins resulting in less PI3K membrane localization [ 15 ]. (biomedcentral.com)

Furthermore, membrane-bound second messengers, i.e., diacylglycerol and D3-phosphorylated phosphatidylinosites, activate proteins kinase C kinases and Akt/PKB kinases, respectively. (pkc-inhibitor.com)

This gene encodes one of the three members of the human AKT serine-threonine protein kinase family which are often referred to as protein kinase B alpha, beta, and gamma. (senescence.info)

AKT proteins are recruited to the cell membrane by phosphatidylinositol 3,4,5-trisphosphate (PIP3) after phosphorylation of phosphatidylinositol 4,5-bisphosphate (PIP2) by PI3K. (senescence.info)

However, phosphorylation sites of PIK3CA/p110α and their underlying mechanism in tumorigenesis are largely unknown. (biomedcentral.com)

Kinase deregulation can contribute to the growth of cancer. (callaix.com)

Drugs given to stop kinases can slow the proliferation of malignant cells and angiogenesis (growth of blood vessels). (callaix.com)

Inappropriate kinase activity triggers a variety of biological cellular responses relating to cell growth, cell differentiation, cell function, survival, apoptosis, and cell mobility implicated in the aforementioned and related diseases. (justia.com)
Apoptosis, proliferation, and differentiation are all affected by phosphorylation. (callaix.com)

This represents a new function for the SAM domain family, which is well characterized for mediating protein-protein interactions. (embl.de)

These proteins are phosphorylated by phosphoinositide 3-kinase (PI3K). (senescence.info)

The resulting unregulated proteolytic activity can reduce protein yield and function. (thermofisher.com)
When these kinases go wrong, normal cellular function can go awry. (callaix.com)
Residues that compose the RNA-binding surface are conserved in a subgroup of SAM domain-containing proteins, suggesting that the function of the domain is conserved from yeast to humans. (embl.de)
There are many known spontaneous or somatic amino acid substitutions and some of these will likely have profound effects on protein function. (ubigene.us)

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)
Phosphorylation can affect protein functions in various ways, like increase or decrease a protein's activity, stabilize it or mark it for destruction, localize it within a specific cellular compartment, and it can initiate or disrupt its interaction with other proteins. (ubigene.us)

We determined the crystal structures of HIPK3 and DYRK1A bound to abemaciclib, showing a similar binding mode to the hinge region of the kinase as observed for Cdk6. (nature.com)

The second messenger PIP3 recruits and activates 3-phosphoinositide dependent protein kinase-1 (PDK1) and AKT serine/threonine kinase on the membrane [ 2 ]. (biomedcentral.com)

Anatomy19

Organisms9

Chemicals and Drugs148

Analytical, Diagnostic and Therapeutic Techniques and Equipment22

Phenomena and Processes54

Information Science3

Receptor9

Phosphatase15

Signal transduction3

Phosphorylate2

Dual specificity4

Receptors3

Vitro kinase2

Intracellular1

Reversible phosphorylation1

Inhibitors12

Amino acids4

Regulate6

Substrate specificity2

Inhibition2

Loss of phosphorylation3

Substrates4

Phosphate6

Enzymes6

RTKs1

T286 in cyclin D11

Pathways4

Degradation3

PDGF1

Broadly1

Conformation5

Regulatory3

Putative protein2

Enzyme1

Catalytic7

JAK11

Ubiquitous1

Mutations1

Regulators1

Post-translationa1

Pleckstrin1

JAKs2

AKT12

Molecular1

Inhibitor compounds2

Pathway4

PTMs4

Localization2

Membrane-bound1

Gene1

Cell membrane1

Mechanism1

Deregulation1

Malignant cells1

Differentiation2

Represents1

PI3K1

Function4

Interaction2

Bound1

PIP31