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Search results 301 to 318 out of 318 for Zap70

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0.017s

Type

Details

Score

Protein Domain

IPR012234 | Tyr_kinase_non-rcpt_SYK/ZAP70

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 non-receptor tyrosine kinases SYK and ZAP-70 [, , ]:SYK is a positive effector of BCR-stimulated responses. It couples the B-cell antigen receptor (BCR) to the mobilisation of calcium ion, either through a phosphoinositide 3-kinase-dependent pathway (when not phosphorylated on tyrosines of the linker region), or through a phospholipase C-gamma-dependent pathway (when phosphorylated on Tyr-342 and Tyr-346). Therefore, the differential phosphorylation of Syk can determine the pathway by which BCR is coupled to the regulation of intracellular calcium ion [, ].ZAP70 plays a role in T-cell development and lymphocyte activation. It is essential for TCR-mediated IL-2 production. Isoform 1 of ZAP70 induces TCR-mediated signal transduction, isoform 2 does not [, ].

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Publication

1423621 | -

First Author:	Chan AC
Year:	1992
Journal:	Cell
Title:	ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain.
Volume:	71
Issue:	4
Pages:	649-62

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Publication

19592646 | J:151601

First Author:	Reeve JL
Year:	2009
Journal:	J Immunol
Title:	SLP-76 couples Syk to the osteoclast cytoskeleton.
Volume:	183
Issue:	3
Pages:	1804-12

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Publication

19670961 | -

First Author:	Ruzza P
Year:	2009
Journal:	Expert Opin Ther Pat
Title:	Therapeutic prospect of Syk inhibitors.
Volume:	19
Issue:	10
Pages:	1361-76

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Publication

8124727 | -

First Author:	Arpaia E
Year:	1994
Journal:	Cell
Title:	Defective T cell receptor signaling and CD8+ thymic selection in humans lacking zap-70 kinase.
Volume:	76
Issue:	5
Pages:	947-58

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Protein

P48025

Organism:	Mus musculus/domesticus
Length:	629
Fragment?:	false

•

Protein

P43404

Organism:	Mus musculus/domesticus
Length:	618
Fragment?:	false

•

Protein

E9PWE9

Organism:	Mus musculus/domesticus
Length:	583
Fragment?:	false

•

Protein

Q6P1E0

Organism:	Mus musculus/domesticus
Length:	629
Fragment?:	false

•

Protein

Q3UPF7

Organism:	Mus musculus/domesticus
Length:	629
Fragment?:	false

•

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

•

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

•

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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