| Type |
Details |
Score |
| Publication |
| First Author: |
Bogin Y |
| Year: |
2007 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
SLP-76 mediates and maintains activation of the Tec family kinase ITK via the T cell antigen receptor-induced association between SLP-76 and ITK. |
| Volume: |
104 |
| Issue: |
16 |
| Pages: |
6638-43 |
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•
•
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| Publication |
| First Author: |
Huang YH |
| Year: |
2007 |
| Journal: |
Science |
| Title: |
Positive regulation of Itk PH domain function by soluble IP4. |
| Volume: |
316 |
| Issue: |
5826 |
| Pages: |
886-9 |
|
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•
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| Publication |
| First Author: |
King PD |
| Year: |
1998 |
| Journal: |
Int Immunol |
| Title: |
CD2-mediated activation of the Tec-family tyrosine kinase ITK is controlled by proline-rich stretch-4 of the CD2 cytoplasmic tail. |
| Volume: |
10 |
| Issue: |
7 |
| Pages: |
1009-16 |
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•
•
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| Publication |
| First Author: |
Jain N |
| Year: |
2013 |
| Journal: |
Nat Med |
| Title: |
CD28 and ITK signals regulate autoreactive T cell trafficking. |
| Volume: |
19 |
| Issue: |
12 |
| Pages: |
1632-7 |
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•
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| Publication |
| First Author: |
Berg LJ |
| Year: |
2007 |
| Journal: |
Nat Rev Immunol |
| Title: |
Signalling through TEC kinases regulates conventional versus innate CD8(+) T-cell development. |
| Volume: |
7 |
| Issue: |
6 |
| Pages: |
479-85 |
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•
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| Publication |
| First Author: |
Prince AL |
| Year: |
2009 |
| Journal: |
Immunol Rev |
| Title: |
The Tec kinases Itk and Rlk regulate conventional versus innate T-cell development. |
| Volume: |
228 |
| Issue: |
1 |
| Pages: |
115-31 |
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•
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| Publication |
| First Author: |
Hong E |
| Year: |
2004 |
| Journal: |
J Biol Chem |
| Title: |
Solution structure and backbone dynamics of the non-receptor protein-tyrosine kinase-6 Src homology 2 domain. |
| Volume: |
279 |
| Issue: |
28 |
| Pages: |
29700-8 |
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•
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| Publication |
| First Author: |
Xiang B |
| Year: |
2008 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Brk is coamplified with ErbB2 to promote proliferation in breast cancer. |
| Volume: |
105 |
| Issue: |
34 |
| Pages: |
12463-8 |
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•
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| Publication |
| First Author: |
Brauer PM |
| Year: |
2010 |
| Journal: |
Biochim Biophys Acta |
| Title: |
Building a better understanding of the intracellular tyrosine kinase PTK6 - BRK by BRK. |
| Volume: |
1806 |
| Issue: |
1 |
| Pages: |
66-73 |
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•
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| Publication |
| First Author: |
Brown K |
| Year: |
2004 |
| Journal: |
J Biol Chem |
| Title: |
Crystal structures of interleukin-2 tyrosine kinase and their implications for the design of selective inhibitors. |
| Volume: |
279 |
| Issue: |
18 |
| Pages: |
18727-32 |
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•
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| Publication |
| First Author: |
Qi Q |
| Year: |
2006 |
| Journal: |
J Biol Chem |
| Title: |
Tec kinase Itk forms membrane clusters specifically in the vicinity of recruiting receptors. |
| Volume: |
281 |
| Issue: |
50 |
| Pages: |
38529-34 |
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•
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| Publication |
| First Author: |
Tsoukas CD |
| Year: |
2006 |
| Journal: |
Adv Exp Med Biol |
| Title: |
Inducible T cell tyrosine kinase (ITK): structural requirements and actin polymerization. |
| Volume: |
584 |
|
| Pages: |
29-41 |
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•
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| Publication |
| First Author: |
Kutach AK |
| Year: |
2010 |
| Journal: |
Chem Biol Drug Des |
| Title: |
Crystal structures of IL-2-inducible T cell kinase complexed with inhibitors: insights into rational drug design and activity regulation. |
| Volume: |
76 |
| Issue: |
2 |
| Pages: |
154-63 |
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| Publication |
| First Author: |
Wu HM |
| Year: |
2012 |
| Journal: |
PLoS One |
| Title: |
Crystal structures of lysine-preferred racemases, the non-antibiotic selectable markers for transgenic plants. |
| Volume: |
7 |
| Issue: |
10 |
| Pages: |
e48301 |
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| Publication |
| First Author: |
Espaillat A |
| Year: |
2014 |
| Journal: |
Acta Crystallogr D Biol Crystallogr |
| Title: |
Structural basis for the broad specificity of a new family of amino-acid racemases. |
| Volume: |
70 |
| Issue: |
Pt 1 |
| Pages: |
79-90 |
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| Publication |
| First Author: |
Alvarez L |
| Year: |
2018 |
| Journal: |
ISME J |
| Title: |
Bacterial secretion of D-arginine controls environmental microbial biodiversity. |
| Volume: |
12 |
| Issue: |
2 |
| Pages: |
438-450 |
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| Publication |
| First Author: |
Radkov AD |
| Year: |
2018 |
| Journal: |
Front Microbiol |
| Title: |
A Broad Spectrum Racemase in Pseudomonas putida KT2440 Plays a Key Role in Amino Acid Catabolism. |
| Volume: |
9 |
|
| Pages: |
1343 |
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•
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| Publication |
| First Author: |
Pan ZQ |
| Year: |
2020 |
| Journal: |
Elife |
| Title: |
Atg1 kinase in fission yeast is activated by Atg11-mediated dimerization and cis-autophosphorylation. |
| Volume: |
9 |
|
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•
|
| Protein Domain |
| Type: |
Family |
| Description: |
The short peptides that forms cross-links between glycan chains in the peptidoglycan polymer in bacterial cell walls require d-amino acids (DAA), being d-Alanine and d-Glutamate the most predominant ones. DAA are generated from the l-enantiomers by specific alanine and glutamate racemases. However, diverse bacteria can produce non-canonical DAA (NCDAA) components of the cell wall, that relies on periplasmic broad-spectrum racemases (Bsr) activity. Lysine racemase is another enzyme present in some organisms and catalyses the conversion of l-Lys to d-Lys but it also can use l-Arg as substrate. Together with Bsr they are classified as Group III racemases []. These NCDAA are involved in different cellular processes including biofilm stability, sporulation and cell communication and allow pathogenic bacteria to adapt in adverse environments []. Sequence studies revealed that Bsr and Lyr contained catalytic Lys and Tyr residues at equivalent positions to that in alanine racemases [, ]. Structural analyses between Bsr from Vibrio cholerae (BsrV) and more restricted enzymes revealed that it exhibits a wider entry site and channel which may facilitate interaction with amino-acid substrates larger than alanine. The catalytic site of BsrV-like racemases is more relaxed that those of related alanine racemases, which is probably due to differences on chamber components and to different interactions of the enzymatic domains to form them [, ]. Crystal structure of Lyr revealed a similar fold of alanine racemases containing an N-terminal α-β barrel and a C-terminal β-stranded domain []. |
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•
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| Protein Domain |
| Type: |
Domain |
| Description: |
In eukaryotes, glutathione S-transferases (GSTs) participate in the detoxification of reactive electrophilic compounds by catalysing theirconjugation to glutathione. The GST domain is also found in S-crystallins from squid, and proteins with no known GST activity, such as eukaryotic elongation factors 1-gamma and the HSP26 family of stress-related proteins, which include auxin-regulated proteins in plants and stringent starvation proteins in Escherichia coli. The major lens polypeptide of Cephalopoda is also a GST [, , , ].Bacterial GSTs of known function often have a specific, growth-supporting role in biodegradative metabolism: epoxide ring opening and tetrachlorohydroquinone reductive dehalogenation are two examples of the reactions catalysed by these bacterial GSTs. Some regulatory proteins, like the stringent starvation proteins, also belong to the GST family [, ]. GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol.Soluble GSTs activate glutathione (GSH) to GS-. In many GSTs, this is accomplished by a Tyr at H-bonding distance from the sulphur of GSH. These enzymes catalyse nucleophilic attack by reduced glutathione (GSH) on nonpolar compounds that contain an electrophilic carbon, nitrogen, or sulphur atom [].Glutathione S-transferases form homodimers, but in eukaryotes can also form heterodimers of the A1 and A2 or YC1 and YC2 subunits. The homodimeric enzymes display a conserved structural fold, with each monomer composed of two distinct domains []. The N-terminal domain forms a thioredoxin-like fold that binds the glutathione moiety, while the C-terminal domain contains several hydrophobic α-helices that specifically bind hydrophobic substrates.This entry represents the N-terminal domain of GST. |
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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 represents serine/threonine-protein kinases (), such as Ulk1 and Ulk2 (Unc-51-Like Kinase). Ulk1 and Ulk2 regulate filopodia extension and branching of sensory axons. They are important for axon growth, playing an essential role in neurite extension of cerebellar granule cells [, ]. |
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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 serine/threonine-protein kinases (), such as Sbk1. Sbk1 may be involved in signal-transduction pathways related to the control of brain development, such as the control of neuronal proliferation or migration in the brain of embryos. |
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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 predicted serine/threonine-protein kinases () such as PknK. |
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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 proteins predicted to be serine/threonine-protein kinases (), such as YKL116C from Saccharomyces cerevisiae (Baker's yeast). |
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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 serine/threonine-protein kinases () with pentapeptide domains, such as SpkB from Synechocystis sp. (strain PCC 6803). SpkB is required for cell motility []. |
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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 numberof diseases [].This enry represents a serine/threonine-protein kinase () found in Asfivirus such as African swine fever virus (ASFV). These enzymes are essential for viral replication and may mediate the virus' progression through DNA replication []. |
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•
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| Protein Domain |
| Type: |
Family |
| Description: |
In eukaryotes, glutathione S-transferases (GSTs) participate in the detoxification of reactive electrophilic compounds by catalysing theirconjugation to glutathione. The GST domain is also found in S-crystallins from squid, and proteins with no known GST activity, such as eukaryotic elongation factors 1-gamma and the HSP26 family of stress-related proteins, which include auxin-regulated proteins in plants and stringent starvation proteins in Escherichia coli. The major lens polypeptide of Cephalopoda is also a GST [, , , ].Bacterial GSTs of known function often have a specific, growth-supporting role in biodegradative metabolism: epoxide ring opening and tetrachlorohydroquinone reductive dehalogenation are two examples of the reactions catalysed by these bacterial GSTs. Some regulatory proteins, like the stringent starvation proteins, also belong to the GST family [, ]. GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol.Soluble GSTs activate glutathione (GSH) to GS-. In many GSTs, this is accomplished by a Tyr at H-bonding distance from the sulphur of GSH. These enzymes catalyse nucleophilic attack by reduced glutathione (GSH) on nonpolar compounds that contain an electrophilic carbon, nitrogen, or sulphur atom [].Glutathione S-transferases form homodimers, but in eukaryotes can also form heterodimers of the A1 and A2 or YC1 and YC2 subunits. The homodimeric enzymes display a conserved structural fold, with each monomer composed of two distinct domains []. The N-terminal domain forms a thioredoxin-like fold that binds the glutathione moiety, while the C-terminal domain contains several hydrophobic α-helices that specifically bind hydrophobic substrates. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
A carbohydrate-binding module (CBM) is defined as a contiguous amino acid sequence within a carbohydrate-active enzyme with a discreet fold having carbohydrate-binding activity. A few exceptions are CBMs in cellulosomal scaffolding proteins and rare instances of independent putative CBMs. The requirement of CBMs existing as modules within larger enzymes sets this class of carbohydrate-binding protein apart from other non-catalytic sugar binding proteins such as lectins and sugar transport proteins.CBMs were previously classified as cellulose-binding domains (CBDs) based on the initial discovery of several modules that bound cellulose [, ]. However, additional modules in carbohydrate-active enzymes are continually being found that bind carbohydrates other than cellulose yet otherwise meet the CBM criteria, hence the need to reclassify these polypeptides using more inclusive terminology.Previous classification of cellulose-binding domains were based on amino acid similarity. Groupings of CBDs were called "Types"and numbered with roman numerals (e.g. Type I or Type II CBDs). In keeping with the glycoside hydrolase classification, these groupings are now called families and numbered with Arabic numerals. Families 1 to 13 are the same as Types I to XIII. For a detailed review on the structure and binding modes of CBMs see [].This entry represents , which binds starch. The crystal structure of CBM20 has been solved []. It consists of seven β-strands forming an open-sided distorted β-barrel. Several aromatic residues, especially the well-conserved Trp and Tyr residues, participate in granular starch binding. |
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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 group represents a protein kinase C, alpha/beta/gamma types. |
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| Protein Domain |
| Type: |
Family |
| 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 a conserved 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 []. |
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| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
The arginine dihydrolase (AD) pathway is found in many prokaryotes and some primitive eukaryotes, an example of the latter being Giardia lamblia (Giardia intestinalis) []. The three-enzyme anaerobic pathway breaks down L-arginine to form 1 mol of ATP, carbon dioxide and ammonia. In simpler bacteria, the first enzyme, arginine deiminase, can account for up to 10% of total cell protein [].Most prokaryotic arginine deiminase pathways are under the control of a repressor gene, termed ArgR []. This is a negative regulator, and will only release the arginine deiminase operon for expression in the presence of arginine []. The crystal structure of apo-ArgR from Bacillus stearothermophilus has been determined to 2.5A by means of X-ray crystallography []. The protein exists as a hexamer of identical subunits, and is shown to have six DNA-binding domains, clustered around a central oligomeric core when bound to arginine. It predominantly interacts with A.T residues in ARG boxes. This hexameric protein binds DNA at its N terminus to repress arginine biosyntheis or activate arginine catabolism. Some species have several ArgR paralogs. In a neighbour-joining tree, some of these paralogous sequences show long branches and differ significantly from the well-conserved C-terminal region. The C-terminal domain of the arginine repressor is responsible for arginine binding and multimerization [, ]. It can also bind ornithine, Pro and Tyr (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). |
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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 the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include catalytic domain of dual specificity 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 of a number of diseases [].Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The DAG kinase domain is assumed to be an accessory domain. Upon cell stimulation, DAG kinase converts DAG into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. It catalyses the reaction: ATP + 1,2-diacylglycerol = ADP +1,2-diacylglycerol 3-phosphate. The enzyme is stimulated by calcium and phosphatidylserine and phosphorylated by protein kinase C. This domain is always associated with . |
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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 domain is found in a large variety of protein kinases with different functions and dependencies. Protein kinase C, for example, is a calcium-activated, phospholipid-dependent serine- and threonine-specific enzyme. It is activated by diacylglycerol which, in turn, phosphorylates a range of cellular proteins. This domain is most often found associated with . |
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| Protein Domain |
| Type: |
Domain |
| Description: |
Human protein-tyrosine kinase-6 (PTK6, also known as breast tumor kinase (Brk)) is a member of the non-receptor protein-tyrosine kinase family and is expressed in two-thirds of all breast tumours []. PTK6 contains an SH3 domain, an SH2 domain, and catalytic domains. For the case of the non-receptor protein-tyrosine kinases, the SH2 domain is typically involved in negative regulation of kinase activity by binding to a phosphorylated tyrosine residue near to the C terminus. The C-terminal sequence of PTK6 (PTSpYENPT where pY is phosphotyrosine) is thought to be a self-ligand for the SH2 domain []. This entry represents the SH2 domain of PTK6. The structure of this domain resembles other SH2 domains except for a centrally located four-stranded antiparallel β-sheet (strands betaA, betaB, betaC, and betaD). There are also differences in the loop length which might be responsible for PTK6 ligand specificity []. There are two possible means of regulation of PTK6: autoinhibitory with the phosphorylation of Tyr playing a role in its negative regulation and autophosphorylation at this site, though it has been shown that PTK6 might phosphorylate signal transduction-associated proteins Sam68 and signal transducing adaptor family member 2 (STAP/BKS) in vivo []. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
Pyruvate carboxylase () (PC), a member of the biotin-dependent enzyme family, is involved in gluconeogenesis by mediating thecarboxylation of pyruvate to oxaloacetate. Biotin-dependent carboxylase enzymes perform a two step reaction. Enzyme-bound biotin is first carboxylated by bicarbonate and ATP and the carboxyl group temporarily bound to biotin is subsequently transferred to an acceptor substrate such as pyruvate []. PC has three functional domains: a biotin carboxylase (BC) domain, a carboxyltransferase (CT) domain which perform the second part of the reaction and a biotinyl domain [, ]. The pyruvate binding to the CT active site induces a conformational change stabilised by the interaction of conserved Asp and Tyr residues in this domain which leads to the formation of the biotin binding pocket and ensures the efficient coupling of BC and CT domain reactions []. The mechanism by which the carboxyl group is transferred from the carboxybiotin to the pyruvate is not well understood.The pyruvate carboxyltransferase domain is also found in other pyruvate binding enzymes and acetyl-CoA dependent enzymes suggesting that this domain can be associated with different enzymatic activities.This domain is found towards the N-terminal region of various aldolase enzymes. This N-terminal TIM barrel domain []interacts with the C-terminal domain. The C-terminal DmpG_comm domain () is thought to promote heterodimerization with members of to form a bifunctional aldolase-dehydrogenase []. |
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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 structureshave been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].This entry represents 3-deoxy-D-manno-octulosonic acid kinase, which is responsible for the ATP-dependent phosphorylation of 3-deoxy-D-manno-octulosonic acid at the 4-OH position during lipopolysaccharide core biosynthesis. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Terminase large subunit (TerL) from bacteriophages and evolutionarily related viruses, is an important component of the DNA packing machinery and comprises an ATPase domain, which powers DNA translocation and a nuclease domain that cuts concatemeric DNA [, , ]. TerL forms pentamers in which the ATPase domains form a ring distal to the capsid. The ATPase domain contains a C-terminal subdomain that sits above the ATPase active site, called the "Lid subdomain"with reference to analogous lid subdomains found in other ATPases []. It contains a hydrophobic patch (Trp and Tyr residues) that mediates critical interactions in the interface between adjacent ATPase subunits and assists the positioning of the arginine finger residue that catalyses ATP hydrolysis []. The endonuclease cuts concatemeric DNA first in the initiation phase in a sequence specific site and later in the completion stage of the DNA packaging process when the capsid is full [, ]. Cryo-EM studies indicate that TerL forms a pentamer that binds to a dodecameric assembly called portal and attaches to the capsid. It has been proposed that nuclease domains form a radially arranged ring that is proximal to portal, playing a key role in pentamer assembly []. The nuclease domain has a RNAse H-like fold and it has been proposed to utilise a two-metal catalysis mechanism like in other RNAse H-like endonucleases such as RNase H, transposases, retroviral integrases and RuvC Holliday junction resolvases []. This entry also includes uncharacterised bacterial sequences. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
PTKs catalyse the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region [, ].Itk is expressed in T-cells and mast cells, and is important in their development and differentiation []. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signalling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization []. It also plays a role in the downstream signalling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4 [, ]. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses []. |
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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 lipopolysaccharide core heptose(I) kinase RfaP, which is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that RfaP is necessary for resistance to hydrophobic and polycationic antimicrobials in Escherichia coli, and that it is required for virulence in invasive strains of S. enterica []. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
The arginine dihydrolase (AD) pathway is found in many prokaryotes and some primitive eukaryotes, an example of the latter being Giardia lamblia (Giardia intestinalis) []. The three-enzyme anaerobic pathway breaks down L-arginine to form 1 mol of ATP, carbon dioxide and ammonia. In simpler bacteria, the first enzyme, arginine deiminase, can account for up to 10% of total cell protein [].Most prokaryotic arginine deiminase pathways are under the control of a repressor gene, termed ArgR []. This is a negative regulator, and will only release the arginine deiminase operon for expression in the presence of arginine []. The crystal structure of apo-ArgR from Bacillus stearothermophilus has been determined to 2.5A by means of X-ray crystallography []. The protein exists as a hexamer of identical subunits, and is shown to have six DNA-binding domains, clustered around a central oligomeric core when bound to arginine. It predominantly interacts with A.T residues in ARG boxes. This hexameric protein binds DNA at its N terminus to repress arginine biosyntheis or activate arginine catabolism. Some species have several ArgR paralogs. In a neighbour-joining tree, some of these paralogous sequences show long branches and differ significantly from the well-conserved C-terminal region. The C-terminal domain of the arginine repressor is responsible for arginine binding and multimerization [, ]. It can also bind ornithine, Pro and Tyr (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). |
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| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents death-associated protein kinases 1 (DAPK1). It act as a positive regulator of apoptosis [, , , , ]. 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 []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Amino acid permeases are integral membrane proteins involved in the transportof amino acids into the cell. A number of such proteins have been found to beevolutionary related [, , ].Aromatic amino acids are concentrated in the cytoplasm of Escherichia coli by 4 distinct transport systems: a general aromatic amino acid permease, and aspecific permease for each of the 3 types (Phe, Tyr and Trp) []. It has been shown []that some permeases in E. coli and related bacteria are evolutionary related.These permeases are proteins of about 400 to 420 amino acids and are located in the cytoplasmic membrane and, like bacterial sugar/cation transporters, are thought to contain 12 transmembrane (TM)regions []- hydropathy analysis, however, is inconclusive, suggesting thepossibility of 10 to 12 membrane-spanning domains []. The best conserved domain is a stretch of 20 residues which seems to be located in a cytoplasmic loop between thefirst and second transmembrane region.This family is specific for aromatic amino acid transporters and includes the tyrosine permease, TyrP (), and the tryptophan transporters TnaB () and Mtr () of E. coli. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
Aromatic ring hydroxylating dioxygenases are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols []. The complex has both hydroxylase and electron transfer components. The hydroxylase component is itself composed of two subunits: an alpha-subunit of about 50kDa, and a beta-subunit of about 20kDa. The electron transfer component is either composed of two subunits: a ferredoxin and a ferredoxin reductase or by a single bifunctional ferredoxin/reductase subunit. Sequence analysis of hydroxylase subunits of ring hydroxylating systems (including toluene, benzene and napthalene 1,2-dioxygenases) suggests they are derived from a common ancestor []. The alpha-subunit binds both a Rieske-like 2Fe-2S cluster and an iron atom: conserved Cys and His residues in the N-terminal region may provide 2Fe-2S ligands, while conserved His and Tyr residues may coordinate the iron. The beta subunit may be responsible for the substrate specificity of the dioxygenase system [].This entry represents the conserved C-terminal domain found in the alpha subunit of aromatic-ring-hydroxylating dioxygenases. It is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands. |
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| Protein Domain |
| Type: |
Binding_site |
| Description: |
Aromatic ring hydroxylating dioxygenases are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols []. The complex has both hydroxylase and electron transfer components. The hydroxylase component is itself composed of two subunits: an alpha-subunit of about 50kDa, and a beta-subunit of about 20kDa. The electron transfer component is either composed of two subunits: a ferredoxin and a ferredoxin reductase or by a single bifunctional ferredoxin/reductase subunit. Sequence analysis of hydroxylase subunits of ring hydroxylating systems (including toluene, benzene and napthalene 1,2-dioxygenases) suggests they are derived from a common ancestor []. The alpha-subunit binds both a Rieske-like 2Fe-2S cluster and an iron atom: conserved Cys and His residues in the N-terminal region may provide 2Fe-2S ligands, while conserved His and Tyr residues may coordinate the iron. The beta subunit may be responsible for the substrate specificity of the dioxygenase system [].The alpha-subunit of the hydroxylase components bind both a 2Fe-2S type iron-sulphur centre and an iron atom. There is, in the N-terminal section of these proteins, a conserved region of 24 residues which contains two cysteines and two histidines which have been shown to be involved in the binding of the iron-sulphur centre []. |
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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 [].The protein kinase D family of enzymes consists of three isoforms: PKD1 (PKCmu), PKD2, and PKD3 (PKCnu). They all share a similar architecture with regulatory sub-domains that play specific roles in the activation, translocation and function of the enzymes. The PKD enzymes have recently been implicated in very diverse cellular functions, including Golgi organisation and plasma membrane directed transport, metastasis, immune responses, apoptosis and cell proliferation []. Each isoform is differentially regulated through phosphorylation []. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
Btk (Bruton tyrosine kinase) is a member of the Tec family, which is a group of nonreceptor tyrosine kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Btk also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain with proline-rich and zinc-binding regions [].Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells [, ]. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor (BCR), leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation []. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis []. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans [, ]. This entry represents the SH3 domain of Btk. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
ITK (also known as Tsk or Emt) is a member of the Tec family, which is a group of nonreceptor tyrosine kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation [], and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. ITK is expressed in T-cells and mast cells, and is important in their development and differentiation [, ]. Of the three Tec kinases expressed in T-cells, ITK plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization []. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28 [], the T-cell surface receptor CD2 [], and the chemokine receptor CXCR4 []. In addition, ITK is crucial for the development of T-helper(Th)2 effector responses []. This entry represents the SH3 domain of ITK. |
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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 domain is found at the C terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain () at their N terminus []. The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers []and is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. |
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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 contains the PknD family of serine/threonine protein kinases which are found in (for example) C. trachomatis. In conjunction with Pkn1 they may play a role in specific interactions with host proteins during intracellular growth []. |
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| Strain |
| Attribute String: |
recombinant inbred (RI) |
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| Strain |
| Attribute String: |
recombinant inbred (RI) |
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| Strain |
| Attribute String: |
recombinant inbred (RI) |
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| Strain |
| Attribute String: |
recombinant inbred (RI) |
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| Strain |
| Attribute String: |
recombinant inbred (RI) |
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| Strain |
| Attribute String: |
recombinant inbred (RI) |
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| Strain |
| Attribute String: |
recombinant inbred (RI) |
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| Genotype |
| Symbol: |
Tyr/Tyr |
| Background: |
involves: 101/Rl * C3H/Rl |
| Zygosity: |
ht |
| Has Mutant Allele: |
true |
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| Publication |
| First Author: |
Favor J |
| Year: |
2001 |
| Journal: |
Genetics |
| Title: |
Molecular characterization of Pax6(2Neu) through Pax6(10Neu): an extension of the Pax6 allelic series and the identification of two possible hypomorph alleles in the mouse Mus musculus. |
| Volume: |
159 |
| Issue: |
4 |
| Pages: |
1689-700 |
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•
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| Publication |
| First Author: |
Gómez-H L |
| Year: |
2016 |
| Journal: |
Nat Commun |
| Title: |
C14ORF39/SIX6OS1 is a constituent of the synaptonemal complex and is essential for mouse fertility. |
| Volume: |
7 |
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| Pages: |
13298 |
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| Publication |
| First Author: |
Calderon A |
| Year: |
2006 |
| Journal: |
Hear Res |
| Title: |
Cochlear developmental defect and background-dependent hearing thresholds in the Jackson circler (jc) mutant mouse. |
| Volume: |
221 |
| Issue: |
1-2 |
| Pages: |
44-58 |
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•
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| Publication |
| First Author: |
Belgardt BF |
| Year: |
2015 |
| Journal: |
Nat Med |
| Title: |
The microRNA-200 family regulates pancreatic beta cell survival in type 2 diabetes. |
| Volume: |
21 |
| Issue: |
6 |
| Pages: |
619-27 |
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•
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| Publication |
| First Author: |
Nobs SP |
| Year: |
2023 |
| Journal: |
Nature |
| Title: |
Lung dendritic-cell metabolism underlies susceptibility to viral infection in diabetes. |
| Volume: |
624 |
| Issue: |
7992 |
| Pages: |
645-652 |
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•
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| Publication |
| First Author: |
Dahan T |
| Year: |
2017 |
| Journal: |
Diabetes |
| Title: |
Pancreatic β-Cells Express the Fetal Islet Hormone Gastrin in Rodent and Human Diabetes. |
| Volume: |
66 |
| Issue: |
2 |
| Pages: |
426-436 |
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•
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| Publication |
| First Author: |
Stickel KC |
| Year: |
2024 |
| Journal: |
Am J Physiol Endocrinol Metab |
| Title: |
Mechanisms of spinophilin-dependent pancreas dysregulation in obesity. |
| Volume: |
327 |
| Issue: |
2 |
| Pages: |
E155-E171 |
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•
•
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| Publication |
| First Author: |
Bossi G |
| Year: |
2005 |
| Journal: |
Traffic |
| Title: |
Normal lytic granule secretion by cytotoxic T lymphocytes deficient in BLOC-1, -2 and -3 and myosins Va, VIIa and XV. |
| Volume: |
6 |
| Issue: |
3 |
| Pages: |
243-51 |
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•
•
|
| Publication |
| First Author: |
Sasaki M |
| Year: |
2017 |
| Journal: |
Diabetes |
| Title: |
Dual Regulation of Gluconeogenesis by Insulin and Glucose in the Proximal Tubules of the Kidney. |
| Volume: |
66 |
| Issue: |
9 |
| Pages: |
2339-2350 |
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•
•
•
|
| Publication |
| First Author: |
Etournay R |
| Year: |
2010 |
| Journal: |
Development |
| Title: |
Cochlear outer hair cells undergo an apical circumference remodeling constrained by the hair bundle shape. |
| Volume: |
137 |
| Issue: |
8 |
| Pages: |
1373-83 |
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•
•
|
| Publication |
| First Author: |
Steinberg SM |
| Year: |
2017 |
| Journal: |
Cancer Res |
| Title: |
Myeloid Cells That Impair Immunotherapy Are Restored in Melanomas with Acquired Resistance to BRAF Inhibitors. |
| Volume: |
77 |
| Issue: |
7 |
| Pages: |
1599-1610 |
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•
•
•
|
| Publication |
| First Author: |
Pytel D |
| Year: |
2016 |
| Journal: |
PLoS Genet |
| Title: |
PERK Is a Haploinsufficient Tumor Suppressor: Gene Dose Determines Tumor-Suppressive Versus Tumor Promoting Properties of PERK in Melanoma. |
| Volume: |
12 |
| Issue: |
12 |
| Pages: |
e1006518 |
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•
•
|
| Publication |
| First Author: |
Dominguez D |
| Year: |
2017 |
| Journal: |
J Immunol |
| Title: |
Exogenous IL-33 Restores Dendritic Cell Activation and Maturation in Established Cancer. |
| Volume: |
198 |
| Issue: |
3 |
| Pages: |
1365-1375 |
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•
•
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| Publication |
| First Author: |
Cheng WC |
| Year: |
2019 |
| Journal: |
Nat Immunol |
| Title: |
Uncoupling protein 2 reprograms the tumor microenvironment to support the anti-tumor immune cycle. |
| Volume: |
20 |
| Issue: |
2 |
| Pages: |
206-217 |
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•
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| Publication |
| First Author: |
Burd CE |
| Year: |
2014 |
| Journal: |
Cancer Discov |
| Title: |
Mutation-specific RAS oncogenicity explains NRAS codon 61 selection in melanoma. |
| Volume: |
4 |
| Issue: |
12 |
| Pages: |
1418-29 |
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•
•
•
•
|
| Publication |
| First Author: |
Monahan KB |
| Year: |
2010 |
| Journal: |
Oncogene |
| Title: |
Somatic p16(INK4a) loss accelerates melanomagenesis. |
| Volume: |
29 |
| Issue: |
43 |
| Pages: |
5809-17 |
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•
•
•
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| Publication |
| First Author: |
Cheng J |
| Year: |
2022 |
| Journal: |
Cell Metab |
| Title: |
Autonomous sensing of the insulin peptide by an olfactory G protein-coupled receptor modulates glucose metabolism. |
| Volume: |
34 |
| Issue: |
2 |
| Pages: |
240-255.e10 |
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•
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| Publication |
| First Author: |
Cerdá-Esteban N |
| Year: |
2017 |
| Journal: |
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