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Search results 801 to 811 out of 811 for Pik3r1

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0.017s

Type

Details

Score

Protein Domain

IPR044124 | ISH2_PIK3R1

Type:

Domain

Description:

Phosphoinositide 3-kinases (PI3Ks) are essential for cell growth, migration, and survival. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit []. p110 is composed of an adaptor-binding domain, a Ras-binding domain, a C2 domain, a helical domain, and a kinase domain. p85 is composed of an SH3 domain, a RhoGap domain, a N-terminal SH2 (nSH2) domain, a inter SH2 (iSH2) domain, and C-terminal (cSH2) domain. There are two inhibitory interactions between p110alpha and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110alpha and 2) p85 iSH2 domain with C2 domain of p110alpha. There are three inhibitory interactions between p110beta and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110beta, 2) p85 iSH2 domain with C2 domain of p110beta, and 3) p85 cSH2 domain with the kinase domain of p110beta []. p110beta is oncogenic as a wild type protein while p110alpha lacks this ability. One explanation is that the regulation of p110beta by p85 is unique because of the addition of inhibitory contacts from the cSH2 domain and the loss of contacts in the iSH2 domain []. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites [].In mammals, there are multiple class IA PI3K regulatory and catalytic subunits. There are three genes that encode at least five different regulatory subunit proteins (p85alpha, p55alpha, p50alpha, p85beta, and p55gamma) and three genes encoding three catalytic subunits (p110alpha, p110beta, and p110delta) [].Among all the class IA PI3K combinations, p85alpha/p110alpha heterodimer has been the most intensely investigated. p110alpha has been shown to be stabilized and inhibited by dimerization with p85alpha []. Moreover, p85alpha (also called PIK3R1) has functions independent of its PI3K regulatory role. It can independently stimulate signalling pathways involved in cytoskeletal rearrangements []. PIK3R1 has been shown to play an important role in insulin signalling [].This entry represents the iSH2 domain found in PIK3R1.

•

Publication

37287451 | J:346337

First Author:	Jing Z
Year:	2023
Journal:	Front Cell Dev Biol
Title:	Epigenetic and transcriptomic alterations in the ClC-3-deficient mice consuming a normal diet.
Volume:	11

Pages:	1196684

•

Publication

21362552 | -

First Author:	Zhang X
Year:	2011
Journal:	Mol Cell
Title:	Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism.
Volume:	41
Issue:	5
Pages:	567-78

•

Publication

19915146 | -

First Author:	Wu H
Year:	2009
Journal:	Proc Natl Acad Sci U S A
Title:	Regulation of Class IA PI 3-kinases: C2 domain-iSH2 domain contacts inhibit p85/p110alpha and are disrupted in oncogenic p85 mutants.
Volume:	106
Issue:	48
Pages:	20258-63

•

Publication

11752634 | -

First Author:	Okkenhaug K
Year:	2001
Journal:	Sci STKE
Title:	New responsibilities for the PI3K regulatory subunit p85 alpha.
Volume:	2001
Issue:	65
Pages:	pe1

•

Publication

17470792 | -

First Author:	Geering B
Year:	2007
Journal:	Proc Natl Acad Sci U S A
Title:	Class IA phosphoinositide 3-kinases are obligate p85-p110 heterodimers.
Volume:	104
Issue:	19
Pages:	7809-14

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Protein

Q80UI5

Organism:	Mus musculus/domesticus
Length:	454
Fragment?:	false

•

Protein

P26450

Organism:	Mus musculus/domesticus
Length:	724
Fragment?:	false

•

Protein

P70304

Organism:	Mus musculus/domesticus
Length:	724
Fragment?:	false

•

Publication

19926274 | -

First Author:	Filippakopoulos P
Year:	2009
Journal:	Curr Opin Struct Biol
Title:	SH2 domains: modulators of nonreceptor tyrosine kinase activity.
Volume:	19
Issue:	6
Pages:	643-9

•

Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

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