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Protein Page:
PIK3R2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PIK3R2 regulatory subunit of phosphoinositide-3-kinase. Mediates binding to a subset of tyrosine-phosphorylated proteins through its SH2 domain. Acts as an adapter, mediating the association of the p110 catalytic unit of the alpha, beta and delta enzymes to the plasma membrane, where p110 phosphorylates inositol lipids. May play an additional role in the regulation of the actin cytoskeleton. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Its SH2 domains interacts with the YTHM motif of phosphorylated INSR in vitro. Defects in PIK3R1 are a cause of severe insulin resistance. Four alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Kinase, lipid
Chromosomal Location of Human Ortholog: 19q13.2-q13.4
Cellular Component: nucleus; cytosol; phosphoinositide 3-kinase complex
Molecular Function: protein binding; protein heterodimerization activity; 1-phosphatidylinositol-3-kinase activity; phosphoinositide 3-kinase regulator activity; receptor tyrosine kinase binding; protein phosphatase binding
Biological Process: epidermal growth factor receptor signaling pathway; phosphoinositide 3-kinase cascade; phosphoinositide-mediated signaling; fibroblast growth factor receptor signaling pathway; nerve growth factor receptor signaling pathway; T cell receptor signaling pathway; regulation of phosphoinositide 3-kinase activity; protein transport; regulation of small GTPase mediated signal transduction; cellular response to insulin stimulus; small GTPase mediated signal transduction; phospholipid metabolic process; insulin receptor signaling pathway; phosphatidylinositol biosynthetic process; positive regulation of transcription factor import into nucleus; cell glucose homeostasis; innate immune response; regulation of autophagy; positive regulation of transcription from RNA polymerase II promoter; blood coagulation; vascular endothelial growth factor receptor signaling pathway; leukocyte migration
Disease: Megalencephaly-polymicrogyria-polydactyly-hydrocephalus Syndrome 1
Reference #:  O00459 (UniProtKB)
Alt. Names/Synonyms: p85; p85-BETA; P85B; Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta; Phosphatidylinositol 3-kinase regulatory subunit beta; phosphatidylinositol 3-kinase, regulatory subunit, polypeptide 2 (p85 beta); phosphoinositide-3-kinase, regulatory subunit 2 (beta); phosphoinositide-3-kinase, regulatory subunit 2 (p85 beta); phosphoinositide-3-kinase, regulatory subunit, polypeptide 2 (p85 beta); PI3-kinase regulatory subunit beta; PI3-kinase subunit p85-beta; PI3K regulatory subunit beta; PIK3R2; PtdIns-3-kinase regulatory subunit beta; PtdIns-3-kinase regulatory subunit p85-beta
Gene Symbols: PIK3R2
Molecular weight: 81,545 Da
Basal Isoelectric point: 6.03  Predict pI for various phosphorylation states
Select Structure to View Below

PIK3R2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S34-p PGDVLVVsRAALQAL
0 6 Y74-p RGDFPGTyVEFLGPV
0 4 R195 PEASAEARRALREAA
0 2 S263-p RAPPPPSsPPPGGAP
0 2 Y365-p SSKIQGEyTLTLRkG
0 1 T366 SKIQGEyTLTLRkGG
0 1 K371-ac EyTLTLRkGGNNkLI
0 1 K376-ac LRkGGNNkLIKVFHR
0 8 Y423-p KLDTRLLyPVSKYQQ
0 11 Y449-p VGAQLKVyHQQyQDK
0 30 Y453-p LKVyHQQyQDKsREy
0 3 S457-p HQQyQDKsREyDQLy
0 14 Y460-p yQDKsREyDQLyEEy
2 1681 Y464-p sREyDQLyEEytRTS
0 170 Y467-p yDQLyEEytRTSQEL
0 13 T468-p DQLyEEytRTSQELQ
0 1 K564-ac DKRMNSLkPDLMQLR
0 15 Y577-p LRKIRDQyLVWLtQK
0 2 T582-p DQyLVWLtQKGARQK
0 2 T601-p WLGIKNEtEDQyALM
0 227 Y605-p KNEtEDQyALMEDED
0 1 A606 NEtEDQyALMEDEDD
0 1 T643 LSGKRDGTFLIRESS
1 1 Y655-p ESSQRGCyACSVVVD
0 1 S658 QRGCyACSVVVDGDT
0 64 Y671-p DTKHCVIyRTATGFG
4228 : Phospho-PI3K p85 (Tyr458)/p55 (Tyr199) Antibody
  mouse

 
S34 PGDLLVVSRVALQAL
Y74 RGDFPGTYVEFLGPV
Y195-p PEAAAEAyRALREVA
- gap
Y359 SSKIQGEYtLTLRKG
T360-p SKIQGEYtLTLRKGG
K365 EYtLTLRKGGNNKLI
K370 LRKGGNNKLIKVFHR
Y417-p KLDTRLLyPVSKYQQ
Y443 VGAQLKVYHQQyQDK
Y447-p LKVYHQQyQDKSREY
S451 HQQyQDKSREYDQLy
Y454 yQDKSREYDQLyEEy
Y458-p SREYDQLyEEyTRTS
Y461-p YDQLyEEyTRTSQEL
T462 DQLyEEyTRTSQELQ
K558 DKRMNSLKPDLMQLR
Y571 LRKIRDQYLVWLTQK
T576 DQYLVWLTQKGARQR
T595 WLGIKNETEDQysLM
Y599-p KNETEDQysLMEDED
S600-p NETEDQysLMEDEDA
T637-p LSGKRDGtFLIRESS
Y649-p ESSQRGCyACsVVVD
S652-p QRGCyACsVVVDGDT
Y665-p DTKHCVIyRTATGFG
4228 : Phospho-PI3K p85 (Tyr458)/p55 (Tyr199) Antibody
  rat

 
S34 PGDLLVVSRVALQAL
Y74-p RGDFPGTyVEFLGPV
Y195 PEAASEAYRAMREVT
- gap
Y359 SSKIQGEYTLTLRKG
T360 SKIQGEYTLTLRKGG
K365 EYTLTLRKGGNNKLI
K370 LRKGGNNKLIKVFHR
Y417 KLDTRLLYPVSKYQQ
Y443 VGAQLKVYHQQYQDK
Y447 LKVYHQQYQDKSREY
S451 HQQYQDKSREYDQLy
Y454 YQDKSREYDQLyEEY
Y458-p SREYDQLyEEYTRTS
Y461 YDQLyEEYTRTSQEL
T462 DQLyEEYTRTSQELQ
K558 DKRMNSLKPDLMQLR
Y571 LRKIRDQYLVWLTQK
T576 DQYLVWLTQKGARQR
T595 WLGIKNETEDQySLM
Y599-p KNETEDQySLMEDED
S600 NETEDQySLMEDEDA
T637 LSAKRDGTFLIRESS
Y649 ESSQRGCYACSVVVD
S652 QRGCYACSVVVDGDT
Y665 DTKHCVIYRTATGFG
4228 : Phospho-PI3K p85 (Tyr458)/p55 (Tyr199) Antibody
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