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Search results 401 to 427 out of 427 for Irs2

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0.041s

Type

Details

Score

Publication

19596999 | J:244680

First Author:	Chang BY
Year:	2009
Journal:	J Immunol
Title:	JAK3 inhibition significantly attenuates psoriasiform skin inflammation in CD18 mutant PL/J mice.
Volume:	183
Issue:	3
Pages:	2183-92

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Publication

7526154 | -

First Author:	Colamonici O
Year:	1994
Journal:	Mol Cell Biol
Title:	Direct binding to and tyrosine phosphorylation of the alpha subunit of the type I interferon receptor by p135tyk2 tyrosine kinase.
Volume:	14
Issue:	12
Pages:	8133-42

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Protein Domain

IPR016251 | Tyr_kinase_non-rcpt_Jak/Tyk2

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 [].Janus kinases (JAKs) are tyrosine kinases that function in membrane-proximal signalling events initiated by a variety of extracellular factors binding to cell surface receptors []. Many type I and II cytokine receptors lack a protein tyrosine kinase domain and rely on JAKs to initiate the cytoplasmic signal transduction cascade. Ligand binding induces oligomerisation of the receptors, which then activates the cytoplasmic receptor-associated JAKs. These subsequently phosphorylate tyrosine residues along the receptor chains with which they are associated. The phosphotyrosine residues are a target for a variety of SH2 domain-containing transducer proteins. Amongst these are the signal transducers and activators of transcription (STAT) proteins, which, after binding to the receptor chains, are phosphorylated by the JAK proteins. Phosphorylation enables the STAT proteins to dimerise and translocate into the nucleus, where they alter the expression of cytokine-regulated genes. This system is known as the JAK-STAT pathway.Four mammalian JAK family members have been identified: JAK1, JAK2, JAK3, and TYK2. They are relatively large kinases of approximately 1150 amino acids, with molecular weights of ~120-130kDa. Their amino acid sequences are characterised by the presence of 7 highly conserved domains, termed JAK homology (JH) domains. The C-terminal domain (JH1) is responsible for the tyrosine kinase function. The next domain in the sequence (JH2) is known as the tyrosine kinase-like domain, as its sequence shows high similarity to functional kinases but does not possess any catalytic activity. Although the function of this domain is not well established, there is some evidence for a regulatory role on the JH1 domain, thus modulating catalytic activity. The N-terminal portion of the JAKs (spanning JH7 to JH3) is important for receptor association and non-catalytic activity, and consists of JH3-JH4, which is homologous to the SH2 domain, and lastly JH5-JH7, which is a FERM domain.This entry represents the non-receptor tyrosine kinases Jak and Tyk2:Jak1 appears to be required in early development for specific cell migrations (epiboly), for the expression of the homeobox protein goosecoid and for the formation of anterior structures [].Jak2 plays a role in leptin signalling and in the control of body weight. It is involved in interleukin-3, and probably interleukin-23, signal transduction [].Jak3 is involved in the interleukin-2 and interleukin-4 signalling pathway. It phosphorylates STAT6, IRS1, IRS2 and PI3K [].Tyk2 is probably involved in intracellular signal transduction by being involved in the initiation of type I IFN signalling. It phosphorylates the interferon-alpha/beta receptor alpha chain [].

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Publication

19290934 | -

First Author:	Ghoreschi K
Year:	2009
Journal:	Immunol Rev
Title:	Janus kinases in immune cell signaling.
Volume:	228
Issue:	1
Pages:	273-87

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Protein

Q8K0I7

Organism:	Mus musculus/domesticus
Length:	632
Fragment?:	true

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Protein

Q62137

Organism:	Mus musculus/domesticus
Length:	1100
Fragment?:	false

•

Protein

P97423

Organism:	Mus musculus/domesticus
Length:	1081
Fragment?:	false

•

Protein

A0A0R4J0R7

Organism:	Mus musculus/domesticus
Length:	1100
Fragment?:	false

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Publication

19275641 | -

First Author:	Sharma PS
Year:	2009
Journal:	Curr Pharm Des
Title:	Receptor tyrosine kinase inhibitors as potent weapons in war against cancers.
Volume:	15
Issue:	7
Pages:	758-76

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Publication

16700535 | -

First Author:	Li E
Year:	2006
Journal:	Biochemistry
Title:	Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies.
Volume:	45
Issue:	20
Pages:	6241-51

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Publication

15845350 | -

First Author:	Roskoski R Jr
Year:	2005
Journal:	Biochem Biophys Res Commun
Title:	Src kinase regulation by phosphorylation and dephosphorylation.
Volume:	331
Issue:	1
Pages:	1-14

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Protein

Q9R117

Organism:	Mus musculus/domesticus
Length:	1184
Fragment?:	false

•

Protein

Q2M4G5

Organism:	Mus musculus/domesticus
Length:	1180
Fragment?:	false

•

Protein

E9QJS1

Organism:	Mus musculus/domesticus
Length:	1207
Fragment?:	false

•

Protein

Q3U447

Organism:	Mus musculus/domesticus
Length:	1207
Fragment?:	false

•

Protein

Q3TDN4

Organism:	Mus musculus/domesticus
Length:	1159
Fragment?:	true

•

Protein

Q3TIS9

Organism:	Mus musculus/domesticus
Length:	1184
Fragment?:	false

•

Protein

P52332

Organism:	Mus musculus/domesticus
Length:	1153
Fragment?:	false

•

Protein

Q62120

Organism:	Mus musculus/domesticus
Length:	1132
Fragment?:	false

•

Protein

Q3U8P8

Organism:	Mus musculus/domesticus
Length:	1126
Fragment?:	false

•

Protein

Q3URU8

Organism:	Mus musculus/domesticus
Length:	1153
Fragment?:	false

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Protein

B1ASP2

Organism:	Mus musculus/domesticus
Length:	1153
Fragment?:	false

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Publication

3291115 | J:31015

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

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Publication

12368087 | -

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

12471243 | -

First Author:	Manning G
Year:	2002
Journal:	Science
Title:	The protein kinase complement of the human genome.
Volume:	298
Issue:	5600
Pages:	1912-34

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Publication

15078142 | -

First Author:	Stout TJ
Year:	2004
Journal:	Curr Pharm Des
Title:	High-throughput structural biology in drug discovery: protein kinases.
Volume:	10
Issue:	10
Pages:	1069-82

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Publication

15320712 | -

First Author:	Li B
Year:	2004
Journal:	Comb Chem High Throughput Screen
Title:	Creating chemical diversity to target protein kinases.
Volume:	7
Issue:	5
Pages:	453-72

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