| Type |
Details |
Score |
| Publication |
| First Author: |
Yu JS |
| Year: |
1995 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Phosphorylation/activation of phosphorylase b kinase by cAMP/Ca2(+)-independent, autophosphorylation-dependent protein kinase. |
| Volume: |
207 |
| Issue: |
1 |
| Pages: |
140-7 |
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•
•
•
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| Publication |
| First Author: |
Zemskova MA |
| Year: |
1995 |
| Journal: |
Biokhimiia |
| Title: |
[Association of rabbit skeletal muscle phosphorylase kinase with sarcoplasmic reticulum membranes]. |
| Volume: |
60 |
| Issue: |
11 |
| Pages: |
1903-10 |
|
•
•
•
•
•
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| Publication |
| First Author: |
Polishchuk SV |
| Year: |
1995 |
| Journal: |
FEBS Lett |
| Title: |
Does phosphorylase kinase control glycogen biosynthesis in skeletal muscle? |
| Volume: |
362 |
| Issue: |
3 |
| Pages: |
271-5 |
|
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•
•
•
•
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| Publication |
| First Author: |
Kagalwalla AF |
| Year: |
1995 |
| Journal: |
J Pediatr |
| Title: |
Phosphorylase b kinase deficiency glycogenosis with cirrhosis of the liver. |
| Volume: |
127 |
| Issue: |
4 |
| Pages: |
602-5 |
|
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•
•
•
•
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| Publication |
| First Author: |
Sahin G |
| Year: |
1998 |
| Journal: |
Neuropediatrics |
| Title: |
Infantile muscle phosphorylase-b-kinase deficiency. A case report. |
| Volume: |
29 |
| Issue: |
1 |
| Pages: |
48-50 |
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•
•
•
•
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| Publication |
| First Author: |
Laforêt P |
| Year: |
1996 |
| Journal: |
Rev Neurol (Paris) |
| Title: |
[Exercise intolerance caused by muscular phosphorylase kinase deficiency. Contribution of in vivo metabolic studies]. |
| Volume: |
152 |
| Issue: |
6-7 |
| Pages: |
458-64 |
|
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•
•
•
•
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| Publication |
| First Author: |
Bebeacua C |
| Year: |
2013 |
| Journal: |
J Virol |
| Title: |
Structure, adsorption to host, and infection mechanism of virulent lactococcal phage p2. |
| Volume: |
87 |
| Issue: |
22 |
| Pages: |
12302-12 |
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•
•
•
•
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| Publication |
| First Author: |
Marchand I |
| Year: |
2001 |
| Journal: |
Mol Microbiol |
| Title: |
Bacteriophage T7 protein kinase phosphorylates RNase E and stabilizes mRNAs synthesized by T7 RNA polymerase. |
| Volume: |
42 |
| Issue: |
3 |
| Pages: |
767-76 |
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•
•
•
•
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| Publication |
| First Author: |
Beppu H |
| Year: |
2005 |
| Journal: |
Genesis |
| Title: |
Generation of a floxed allele of the mouse BMP type II receptor gene. |
| Volume: |
41 |
| Issue: |
3 |
| Pages: |
133-7 |
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•
•
•
•
•
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| Publication |
| First Author: |
Beppu H |
| Year: |
2004 |
| Journal: |
Am J Physiol Lung Cell Mol Physiol |
| Title: |
BMPR-II heterozygous mice have mild pulmonary hypertension and an impaired pulmonary vascular remodeling response to prolonged hypoxia. |
| Volume: |
287 |
| Issue: |
6 |
| Pages: |
L1241-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Roberts KE |
| Year: |
2004 |
| Journal: |
Eur Respir J |
| Title: |
BMPR2 mutations in pulmonary arterial hypertension with congenital heart disease. |
| Volume: |
24 |
| Issue: |
3 |
| Pages: |
371-4 |
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•
•
•
•
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| Publication |
| First Author: |
Zhicheng J |
| Year: |
2004 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Bone morphogenetic protein receptor-II mutation Arg491Trp causes malignant phenotype of familial primary pulmonary hypertension. |
| Volume: |
315 |
| Issue: |
4 |
| Pages: |
1033-8 |
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•
•
•
•
•
|
| Publication |
| First Author: |
West J |
| Year: |
2004 |
| Journal: |
Circ Res |
| Title: |
Pulmonary hypertension in transgenic mice expressing a dominant-negative BMPRII gene in smooth muscle. |
| Volume: |
94 |
| Issue: |
8 |
| Pages: |
1109-14 |
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•
•
•
•
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| Publication |
| First Author: |
Beppu H |
| Year: |
2000 |
| Journal: |
Dev Biol |
| Title: |
BMP type II receptor is required for gastrulation and early development of mouse embryos. |
| Volume: |
221 |
| Issue: |
1 |
| Pages: |
249-58 |
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•
•
•
•
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| Publication |
| First Author: |
Délot EC |
| Year: |
2003 |
| Journal: |
Development |
| Title: |
BMP signaling is required for septation of the outflow tract of the mammalian heart. |
| Volume: |
130 |
| Issue: |
1 |
| Pages: |
209-20 |
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•
•
•
•
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| Publication |
| First Author: |
Toshima J |
| Year: |
1995 |
| Journal: |
J Biol Chem |
| Title: |
Identification and characterization of a novel protein kinase, TESK1, specifically expressed in testicular germ cells. |
| Volume: |
270 |
| Issue: |
52 |
| Pages: |
31331-7 |
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•
•
•
•
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| Publication |
| First Author: |
Toshima J |
| Year: |
1999 |
| Journal: |
J Biol Chem |
| Title: |
Dual specificity protein kinase activity of testis-specific protein kinase 1 and its regulation by autophosphorylation of serine-215 within the activation loop. |
| Volume: |
274 |
| Issue: |
17 |
| Pages: |
12171-6 |
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•
•
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| Publication |
| First Author: |
Toshima J |
| Year: |
2001 |
| Journal: |
Mol Biol Cell |
| Title: |
Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation. |
| Volume: |
12 |
| Issue: |
4 |
| Pages: |
1131-45 |
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•
•
•
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| Publication |
| First Author: |
Leeksma OC |
| Year: |
2002 |
| Journal: |
Eur J Biochem |
| Title: |
Human sprouty 4, a new ras antagonist on 5q31, interacts with the dual specificity kinase TESK1. |
| Volume: |
269 |
| Issue: |
10 |
| Pages: |
2546-56 |
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•
•
•
•
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| Publication |
| First Author: |
Tsumura Y |
| Year: |
2005 |
| Journal: |
Biochem J |
| Title: |
Sprouty-4 negatively regulates cell spreading by inhibiting the kinase activity of testicular protein kinase. |
| Volume: |
387 |
| Issue: |
Pt 3 |
| Pages: |
627-37 |
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•
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| Publication |
| First Author: |
Bottaro DP |
| Year: |
1991 |
| Journal: |
Science |
| Title: |
Identification of the hepatocyte growth factor receptor as the c-met proto-oncogene product. |
| Volume: |
251 |
| Issue: |
4995 |
| Pages: |
802-4 |
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•
•
•
•
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| Publication |
| First Author: |
Wang MH |
| Year: |
1994 |
| Journal: |
Science |
| Title: |
Identification of the ron gene product as the receptor for the human macrophage stimulating protein. |
| Volume: |
266 |
| Issue: |
5182 |
| Pages: |
117-9 |
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•
•
•
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| Publication |
| First Author: |
Maruyama T |
| Year: |
2007 |
| Journal: |
Clin Exp Immunol |
| Title: |
Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells. |
| Volume: |
147 |
| Issue: |
1 |
| Pages: |
164-75 |
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•
•
•
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| Publication |
| First Author: |
Shiba T |
| Year: |
2013 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Structure of the trypanosome cyanide-insensitive alternative oxidase. |
| Volume: |
110 |
| Issue: |
12 |
| Pages: |
4580-5 |
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| Protein Domain |
| Type: |
Conserved_site |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].This entry represents RIO kinase, they exhibit little sequence similarity with eukaryotic protein kinases, and are classified as atypical protein kinases []. The conformation of ATP when bound to the RIO kinases is unique when compared with ePKs, such as serine/threonine kinases or the insulin receptor tyrosine kinase, suggesting that the detailed mechanism by which the catalytic aspartate of RIO kinases participates in phosphoryl transfer may not be identical to that employed in known serine/threonine ePKs. Representatives of the RIO family are present in organisms varying from Archaea to humans, although the RIO3 proteins have only been identified in multicellular eukaryotes, to date. Yeast Rio1 and Rio2 proteins are required for proper cell cycle progression and chromosome maintenance, and are necessary for survival of the cells. These proteins are involved in the processing of 20 S pre-rRNA via late 18 S rRNA processing. |
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•
•
•
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| Protein Domain |
| Type: |
Domain |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases []. |
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•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases [].This group represents a membrane-associated tyrosine- and threonine-specific Cdc2-inhibitory kinase. |
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•
•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases [].This group represents a tyrosine-protein kinase, Ret receptor type. |
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•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases [].This group represents a group of known and predicted receptor-type tyrosine-protein kinases, including the EGF and ERB receptors, and the melanoma-inducing oncogene product XmrK. |
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•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases [].This entry represents the receptor tyrosine kinases for HGF (hepatocyte growth factor) and MSP (macrophage-stimulating protein) []. The HGF receptor functions in cell proliferation, scattering, morphogenesis and survival [, ]. |
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•
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| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases [].This entry represents Fes/Fps family of non-receptor tyrosine kinases. |
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•
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| Protein Domain |
| Type: |
Domain |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments ofa number of diseases [].Eukaryotic protein kinases [, , , , ]are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residue which is important for the catalytic activity of the enzyme [].This entry represents the protein kinase domain containing the catalytic function of protein kinases []. This domain is found in serine/threonine-protein kinases, tyrosine-protein kinases and dual specificity protein kinases. |
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•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].This entry represents a protein encoded by the bacteriophage T7 early gene 0.7. This gene is dispensible in a fast-growing host, but is essential when the host is growing suboptimally. The protein is bifunctional, with the C-terminal third involved in host transcription shut-off, while the N-terminal two-thirds has protein kinase activity and is capable of phosphorylating a number of host cell proteins and itself []. Expression of the protein kinase in the host leads to the phosphorylation of host RNAse E and the stabilisation of phage mRNA. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Phosphorylase B kinase () belongs to a family of proteins involved in glycogen biosynthesis []. The protein has a subunit compositionof (alpha, beta, gamma, delta)4, where the alpha and beta subunits are regulatory, delta is calmodulin, and the gamma subunit is catalytic. The enzyme is believed to have a dual role, the first is connected with glycogendegradation via phosphorylation of glycogen phosphorylase; the second controls glycogen biosynthesis on the sarcoplasmic reticular membrane moredirectly by phosphorylation, and thus inhibition, of glycogen synthase [].The gamma catalytic chain contains three domains; one protein kinase and twocalmodulin-binding domains. Calcium and magnesium ions, together with cyclicAMP, positively affect the efficiency of the enzyme, which is believed to be associated with its auto-kinase activity [, ].The full extent of the effects of deficiencies in this enzyme in humans is unknown; but case studies have been documented [, , ]that detail symptoms asmild as 'exercise intolerance' [], to infant mortality arising from floppyinfant syndrome []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Angiotensin II is a blood-borne hormone produced in the circulation, it is also formed in many tissues such as the brain, kidney, heart, and blood vessels, where angiotensin II functions as a paracrine and autocrine hormone. The known actions of angiotensin II are mediated through two angiotensin receptor subtypes, Angiotensin II receptor 1 and angiotensin II receptor 2, which are members of the seven transmembrane rhodopsin-like G-protein coupled receptor family. These subtypes are important in the renin-angiotensin system, as they are responsible for the signal transduction of the vasoconstricting stimulus of the main effector hormone, angiotensin II []. They also stimulate increased fluid intake and regulate the neuroendocrine system [].This entry represents angiotensin II receptor type 2 (AT2), which plays an important role in the CNS and cardiovascular functions mediated by the renin-angiotensin system. The AT2 receptor is highly expressed in various foetal tissues, with lower levels in the brain and reproductive tissues []. It appears to be up-regulated after vascular injury, myocardial infarction, cardiac failure or wound healing [, , , ]. Depending on the tissue type, activation of the AT2 receptor also appears to stimulate intracellular mechanisms involving Tyr and Ser/Thr phosphatases, which leads to the inactivation of the AT1 and growth factor activated kinases [, , , , , , ]. However, when inducing cell differentiation, the AT2 receptor can also stimulate MAP kinases Erk1/Erk2 []. As a consequence, there is an inactivation of MAP kinase, promotion of apoptosis, repolarization trough opening of delayed-rectifier K+ channels and calcium and voltage activated potassium channel, closing of T -type Ca2+ channels and vasodilation [, , , ]. Through its phosphatase activity, the AT2 receptor regulates the NF-kappaB pathway [, ]and interferes with the inflammatory process [, ]. The AT2 receptor does not require receptor phosphorylation or heterotrimeric G alpha/beta/gamma protein to be active []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].MAP (Mitogen Activated Protein) kinases participate in kinase cascades,whereby at least 3 protein kinases act in series, culminatingin activationof MAP kinase []. MAP kinases are activated by dual phosphorylationon both tyrosine and threonine residues of a conserved TXY motif.p38 proteins belong to the MAP kinase family and were discovered in 3different contexts independently: first, as tyrosine phosphoproteins foundin extracts of cells treated with inflammatory cytokines; second, astargets of a pyrinidyl imidazole drug that blocks production of TNFalpha; and third, as reactivating kinases for MAP kinase-activated protein(MAPKAP) []. The proteins are activated by cytokines, hormones, GPCRs,osmotic shock, heat shock and other stresses []. |
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•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
The alternative oxidase (AOX) is an enzyme that forms part of the electron transport chain in mitochondria of different organisms [, ]. Proteins homologous to the mitochondrial oxidase have also been identified in bacterial genomes [, ]. The oxidase provides an alternative route for electrons passing through the electron transport chain to reduce oxygen. However, as several proton-pumping steps are bypassed in this alternative pathway, activation of the oxidase reduces ATP generation. This enzyme was first identified as a distinct oxidase pathway from cytochrome c oxidase as the alternative oxidase is resistant to inhibition by the poison cyanide [].The alternative oxidase (also known as ubiquinol oxidase) is used as a second terminal oxidase in the mitochondria, electrons are transferred directly from reduced ubiquinol to oxygen forming water []. This is not coupled to ATP synthesis and is not inhibited by cyanide, this pathway is a single step process []. In Oryza sativa (rice) the transcript levels of the alternative oxidase are increased by low temperature []. It has been predicted to contain a coupled diiron centre on the basis of aconserved sequence motif consisting of the proposed iron ligands, four Glu and two His residues []. The EPR study of Arabidopsis thaliana (mouse-ear cress) alternative oxidase AOX1a shows that the enzyme contains a hydroxo-bridged mixed-valent Fe(II)/Fe(III) binuclear iron centre []. A catalytic cycle has been proposed that involves a di-iron centre and at least one transient protein-derived radical, most probably an invariant Tyr residue [].The structure of alternative oxidase from Trypanosoma brucei has been solved. The enzyme is a homodimer with the nonhaem di-iron carboxylate active site buried within a four-helix bundle. In the inhibitor-free state, the di-iron carboxylate is ligated by four glutamate residues, but on binding of an inhibitor, a histidine is also induced to act as a ligand. A highly conserved tyrosine is close to the active site and required for activity []. This entry represents proteins with a structure similar to that of alternative oxidase. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Bone morphogenetic proteins (BMPs) regulate a wide range of cellular functions that contribute to embryonic development from mesoderm formation to organogenesis []. BMP type II receptor (BMPR2) transduces BMP signals from all BMPs by forming heteromeric complexes with and phosphorylating BMP type I receptors. Heterozygous germline mutations of BMPR-II gene in mice []complement the finding of BMPR-II mutations in patients with familial and sporadic primary pulmonary hypertension, indicating that BMPR-II may contribute to the maintenance of normal pulmonary vascular structure and function [, ].Mice with a smooth muscle-specific transgenic mouse expressing a dominant-negative BMPR-II under control of the tetracycline develop pulmonary hypertension []. Knockout studies have demonstrated that BMPR-II is essential for epiblast differentiation and mesoderm induction during early mouse development []. In contrast, knockout mice that express a BMPR-II lacking half of the ligand-binding domain die at midgestation with cardiovascular and skeletal defects []. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].This entry represents RIO kinase, they exhibit little sequence similarity with eukaryotic protein kinases, and are classified as atypical protein kinases []. The conformation of ATP when bound to the RIO kinases is unique when compared with ePKs, such as serine/threonine kinases or the insulin receptor tyrosine kinase, suggesting that the detailed mechanism by which the catalytic aspartate of RIO kinases participates in phosphoryl transfer may not be identical to that employed in known serine/threonine ePKs. Representatives of the RIO family are present in organisms varying from Archaea to humans, although the RIO3 proteins have only been identified in multicellular eukaryotes, to date. Yeast Rio1 and Rio2 proteins are required for proper cell cycle progression and chromosome maintenance, and are necessary for survival of the cells. These proteins are involved in the processing of 20 S pre-rRNA via late 18 S rRNA processing. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].This entry represents the salt-inducible protein kinases, SIK1 and SIK2, which are serine/threonine-protein kinases primarily activated by the master kinase LKB1 (STK11). SIK1 is involved in a variety of processes, such as cell cycle regulation, gluconeogenesis and lipogenesis regulation and muscle growth [, , , ]. SIK2 phosphorylates insulin receptor substrate-1 (IRS1) in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction, and may have a role in the development of insulin resistance in diabetes [. SIK1/2 inhibit CREB activity by phosphorylating and inhibiting activity of TORCs, the CREB-specific coactivators, like CRTC2/TORC2 and CRTC3/TORC3 in response to cAMP signalling []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Binding_site |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Eukaryotic protein kinases [, , , , ]are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases.This entry represents a conserved site, which is located in the N-terminal extremity of the catalytic domain, where there is a glycine-rich stretch of residues in the vicinity of a lysine residue. It is this lysine residue that has been shown to be involved in ATP binding. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Eukaryotic protein kinases [, , , ]are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases.This group of genes codes for 9-kb striated preferentially expressed gene (SPEG)alpha and the 11-kb SPEGbeta found in skeletal muscle and heart. SPEGbeta encodes a 355kDa protein that contains two serine/threonine kinase domains and is homologous to proteins of the myosin light chain kinase family. At least one kinase domain is active and capable of autophosphorylation []. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].TESK1 (testis-specific protein kinase 1) is a protein kinase with a structure composed of an N-terminal protein kinase domain and a C-terminal proline-rich domain and is most closely related to the LIM motif-containing protein kinase (LIMK) subfamily []. TESK1 has kinase activity with dual specificity on both serine/threonine and tyrosine residues []. When expressed in HeLa cells, TESK1 stimulates the formation of actin stress fibres and focal adhesions and functions downstream of integrins through phosphorylation and inactivation of cofilin []. In a yeast two-hybrid screen, Sprouty4 was identified as a binding partner of TESK1 [], and was subsequently found to negatively regulate cell spreading by inhibiting the kinase activity of TESK1 []. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents a domain found in various ephrin type A and B receptors, which have tyrosine kinase activity.Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specificinhibitors for the treatments of a number of diseases [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases []. |
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•
•
•
•
|
| Protein Domain |
| Type: |
Active_site |
| Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse thetransfer 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Eukaryotic protein kinases [, , , ]are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in thevicinity of a lysine residue, which has been shown to be involved in ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residue, which is important for the catalytic activity of the enzyme []. This signature contains the active site aspartate residue. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
417
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
332
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
414
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
75
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
289
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
202
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
332
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
315
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
202
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
203
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
90
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
454
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
67
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
182
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
417
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
315
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jörnvall H |
| Year: |
1995 |
| Journal: |
Biochemistry |
| Title: |
Short-chain dehydrogenases/reductases (SDR). |
| Volume: |
34 |
| Issue: |
18 |
| Pages: |
6003-13 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ehmann DE |
| Year: |
1999 |
| Journal: |
Biochemistry |
| Title: |
Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5. |
| Volume: |
38 |
| Issue: |
19 |
| Pages: |
6171-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Maltais LJ |
| Year: |
1994 |
| Journal: |
Mouse Genome |
| Title: |
Locus Map of mouse |
| Volume: |
92 |
|
| Pages: |
62-85 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
358
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
380
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
485
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
863
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
525
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
367
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
465
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
464
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
431
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
627
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
411
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
291
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
525
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
409
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
434
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
335
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
368
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
260
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
352
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
671
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
392
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
380
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
500
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
464
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
353
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
348
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
368
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
211
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
268
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
404
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
417
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1210
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1210
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hanks SK |
| Year: |
1988 |
| Journal: |
Science |
| Title: |
The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. |
| Volume: |
241 |
| Issue: |
4861 |
| Pages: |
42-52 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Manning G |
| Year: |
2002 |
| Journal: |
Trends Biochem Sci |
| Title: |
Evolution of protein kinase signaling from yeast to man. |
| Volume: |
27 |
| Issue: |
10 |
| Pages: |
514-20 |
|
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•
•
•
•
|
| Publication |
| First Author: |
Manning G |
| Year: |
2002 |
| Journal: |
Science |
| Title: |
The protein kinase complement of the human genome. |
| Volume: |
298 |
| Issue: |
5600 |
| Pages: |
1912-34 |
|
•
•
•
•
•
|
