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PIK3R2 (human)

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 Cellular Component: cytosol; phosphoinositide 3-kinase complex Molecular Function: protein binding; 1-phosphatidylinositol-3-kinase activity; phosphoinositide 3-kinase regulator activity; receptor tyrosine kinase binding Biological Process: platelet activation; regulation of small GTPase mediated signal transduction; phosphoinositide-mediated signaling; nerve growth factor receptor signaling pathway; phospholipid metabolic process; small GTPase mediated signal transduction; T cell costimulation; phosphatidylinositol biosynthetic process; insulin receptor signaling pathway; blood coagulation; leukocyte migration; T cell receptor signaling pathway 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 CST Pathways:  Adherens Junction Dynamics  |  AMPK Signaling  |  Angiogenesis  |  Apoptosis  |  B Cell Receptor Signaling  |  ErbB/HER Signaling  |  ESC Pluripotency and Differentiation  |  Inhibition of Apoptosis  |  Insulin Receptor Signaling  |  Jak/Stat/IL-6 Signaling  |  MAPK/Erk in Growth and Differentiation  |  Mitochondrial Control of Apoptosis  |  mTOR Signaling  |  NF-kB Signaling  |  PI3K/Akt Signaling  |  Protein Kinase C Signaling  |  Regulation of Actin Dynamics  |  Regulation of Microtubule Dynamics  |  SAPK/JNK Signaling Cascades  |  T Cell Receptor Signaling  |  TGF-ß Signaling  |  Translation: eIF4E and p70S6K  |  Warburg Effect

Select Structure to View Below PIK3R2 2KT1 - A=1-80 (human) 2XS6 - A=108-298 (human) 3MTT - A=433-610 (human) 3O5Z - A/B=1-85 (human) 2Y3A - B=423-722 (mouse)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 2KT1 2XS6 3MTT 3O5Z  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	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

SS  SS: 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.	MS  MS: 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	1		S263-p	RAPPPPSsPPPGGAP
0	2		Y365-p	SSKIQGEyTLTLRkG
0	1		K371-a	EyTLTLRkGGNNkLI
0	1		K376-a	LRkGGNNkLIKVFHR
0	7		Y423-p	KLDTRLLyPVSKYQQ
0	11		Y449-p	VGAQLKVyHQQyQDK
0	31		Y453-p	LKVyHQQyQDKsREy
0	3		S457-p	HQQyQDKsREyDQLy
0	13		Y460-p	yQDKsREyDQLyEEy
1	1709		Y464-p	sREyDQLyEEytRTS
0	173		Y467-p	yDQLyEEytRTSQEL
0	13		T468-p	DQLyEEytRTSQELQ
0	1		K564-a	DKRMNSLkPDLMQLR
0	11		Y577-p	LRKIRDQyLVWLtQK
0	1		T582-p	DQyLVWLtQKGARQK
0	1		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

	mouse
S34	PGDLLVVSRVALQAL
Y74	RGDFPGTYVEFLGPV
Y195-p	PEAAAEAyRALREVA
-	gap
Y359	SSKIQGEYTLTLRKG
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

	rat
S34	PGDLLVVSRVALQAL
Y74-p	RGDFPGTyVEFLGPV
Y195	PEAASEAYRAMREVT
-	gap
Y359	SSKIQGEYTLTLRKG
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

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