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Protein Domain : IPR001720

Name  PI3 kinase, P85 regulatory subunit Short Name  PI3kinase_P85
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 [].PI3 kinases are enzymes that phosphorylate phosphoinositides on the 3-hydroxyl group of the inositol ring. The precise functions of the three products of PI3 kinase (PI-3-P, PI-3,4-P and PI-3,4,5-P) are not yet known, but it is suggested that they function as second messengers in signal transduction events in organisms ranging from yeast to mammals. There are several forms of PI3 kinase. One of these is the mammalian enzyme, a heterodimer of a 110 kDa catalytic subunit and an 85 kDa regulatory subunit, which allows it to bind to activated tyrosine protein kinases. PI3 kinase P85 alpha subunits contain an N-terminal SH3 domain, and two SH2 domains in the C-terminal half of the sequence [, ].

Publication Counts Displayer

0 Child Features

2 Contains

DB identifier Name Short Name Type
IPR000980 SH2 domain SH2 Domain
IPR001452 SH3 domain SH3_domain Domain

2 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PTHR10155 PANTHER IPR001720
PR00678 PRINTS IPR001720

3 Data Sets

Name URL
TrEMBL data set http://www.ebi.ac.uk/trembl/
InterPro data set  
InterPro GO Annotation data set  

0 Found In

2 GO Annotation


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
PI3 kinase, P85 regulatory subunit   GO:0035014 phosphatidylinositol 3-kinase regulator activity
PI3 kinase, P85 regulatory subunit   GO:0005942 phosphatidylinositol 3-kinase complex

2 Ontology Annotations


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
PI3 kinase, P85 regulatory subunit   GO:0035014 phosphatidylinositol 3-kinase regulator activity
PI3 kinase, P85 regulatory subunit   GO:0005942 phosphatidylinositol 3-kinase complex

0 Parent Features

19 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0303633 M9PAY7 Drosophila melanogaster
FBpp0303632 Q7KTZ2 Drosophila melanogaster
FBpp0278911 Q29NX3 Drosophila pseudoobscura
FBpp0166255 B4KHH3 Drosophila mojavensis
FBpp0239106 B4LU46 Drosophila virilis
FBpp0261746 B4P2C7 Drosophila yakuba
A8XBV2_CAEBR A8XBV2 Caenorhabditis briggsae
A8WVQ7_CAEBR A8WVQ7 Caenorhabditis briggsae
H2WJI7_CAEJA H2WJI7 Caenorhabditis japonica
G0P6D4_CAEBE G0P6D4 Caenorhabditis brenneri
G0MF51_CAEBE G0MF51 Caenorhabditis brenneri
G0P8K0_CAEBE G0P8K0 Caenorhabditis brenneri
G0MGT1_CAEBE G0MGT1 Caenorhabditis brenneri
G5EDP9_CAEEL G5EDP9 Caenorhabditis elegans
G5ECJ6_CAEEL G5ECJ6 Caenorhabditis elegans
V6CL92_CAEEL V6CL92 Caenorhabditis elegans
O18683_DROME O18683 Drosophila melanogaster
E3M3J7_CAERE E3M3J7 Caenorhabditis remanei
E3MX87_CAERE E3MX87 Caenorhabditis remanei