Protein Domain : IPR023420

Type:  Domain Name:  Tyrosine-protein kinase SYK/ZAP-70, inter-SH2 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 [].SYK is a positive effector of B-cell antigen receptor (BCR) stimulated responses [, ]. ZAP-70 plays a role in T-cell development and lymphocyte activation. It is essential for TCR-mediated IL-2 production [, ].The N-terminal region of ZAP-70 consists of two SH2 domains that are conected by an helical region. The overall fold is Y shaped, with the intervening residues forming the stem []. This entry represents the inter-SH2 domain found in ZAP-70 and SYK kinases. Short Name:  Kinase_SYK/ZAP-70_inter-SH2

0 Child Features

0 Contains

1 Cross References


0 Found In

1 GO Annotation

GO Term Gene Name Organism
GO:0004715 IPR023420

0 Parent Features

24 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
51852.m000019 B9TMB3 PAC:16828459 Ricinus communis 49  
GSVIVT01009436001 PAC:17821851 Vitis vinifera 235  
orange1.1g031310m A0A067H3M5 PAC:18136722 Citrus sinensis 161  
orange1.1g031323m A0A067H3M5 PAC:18136723 Citrus sinensis 161  
Ciclev10022608m V4U909 PAC:20809653 Citrus clementina 161  
Ciclev10022609m V4U909 PAC:20809651 Citrus clementina 161  
Ciclev10022610m V4U909 PAC:20809652 Citrus clementina 161  
Gorai.006G202400.1 A0A0D2NVN6 PAC:26829627 Gossypium raimondii 239  
Gorai.006G202400.2 A0A0D2S6P6 PAC:26829628 Gossypium raimondii 237  
Gorai.006G202400.3 A0A0D2QDK3 PAC:26829629 Gossypium raimondii 205  
Thecc1EG033769t1 A0A061FBF6 PAC:27458867 Theobroma cacao 235  
Brara.E02369.1.p PAC:30624149 Brassica rapa FPsc 588  
Brara.K00310.1.p PAC:30606726 Brassica rapa FPsc 183  
Bostr.2983s0193.1.p PAC:30662832 Boechera stricta 119  
evm_27.model.AmTr_v1.0_scaffold00101.92 W1NV07 PAC:31558306 Amborella trichopoda 279  
Traes_2AL_97834165F.7 PAC:31911015 Triticum aestivum 48  
Manes.01G156600.1.p PAC:32358298 Manihot esculenta 419  
AL6G50390.t1 PAC:35927978 Arabidopsis lyrata 120  
AUR62004281-RA PAC:36319446 Chenopodium quinoa 323  
Bol032780 PAC:37369550 Brassica oleracea capitata 571  
Lsat_1_v5_gn_7_113181.1 PAC:38912782 Lactuca sativa 99  
evm.model.AsparagusV1_08.3417 PAC:40527640 Asparagus officinalis 236  
Sevir.5G468950.2.p PAC:40634713 Setaria viridis 100  
Sevir.5G468950.1.p PAC:40634712 Setaria viridis 100  

13 Publications

First Author Title Year Journal Volume Pages PubMed ID