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PIK3R1 (mouse)

Overview PIK3R1 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; Enzyme, regulatory subunit Cellular Component: neuron projection; protein complex; membrane; cytoplasm; plasma membrane; intracellular; cytosol; nucleus; phosphoinositide 3-kinase complex Molecular Function: protein C-terminus binding; protein domain specific binding; neurotrophin TRKA receptor binding; 1-phosphatidylinositol-3-kinase activity; platelet-derived growth factor receptor binding; phosphoprotein binding; 1-phosphatidylinositol-3-kinase regulator activity; phosphoinositide 3-kinase regulator activity; receptor tyrosine kinase binding; protein kinase binding; protein phosphatase binding; insulin receptor binding; ATPase binding; calmodulin binding; insulin binding; insulin-like growth factor receptor binding; protein binding; ErbB-3 class receptor binding; insulin receptor substrate binding; ubiquitin protein ligase binding; phosphoinositide 3-kinase binding; estrogen receptor binding; kinase activity; receptor binding Biological Process: negative regulation of osteoclast differentiation; phosphoinositide 3-kinase cascade; negative regulation of heart rate; response to cAMP; negative regulation of smooth muscle cell proliferation; positive regulation of apoptosis; response to glucocorticoid stimulus; signal transduction; regulation of phosphoinositide 3-kinase activity; protein amino acid phosphorylation; NFAT protein import into nucleus; response to insulin stimulus; negative regulation of blood pressure; negative regulation of proteolysis; glucose metabolic process; negative regulation of cell-matrix adhesion; positive regulation of myoblast differentiation; insulin-like growth factor receptor signaling pathway; B cell differentiation; insulin receptor signaling pathway; positive regulation of transcription from RNA polymerase II promoter; positive regulation of protein amino acid phosphorylation; negative regulation of cell-cell adhesion; phosphorylation; positive regulation of cell migration; negative regulation of apoptosis Reference #:  P26450 (UniProtKB) Alt. Names/Synonyms: AA414921; C530050K14; p50alpha; p55alpha; P85A; p85alpha; Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha; Phosphatidylinositol 3-kinase regulatory subunit alpha; phosphatidylinositol 3-kinase, regulatory subunit, polypeptide 1 (p85 alpha); PI3-kinase regulatory subunit alpha; PI3-kinase subunit p85-alpha; PI3K; PI3K regulatory subunit alpha; Pik3r1; PtdIns-3-kinase regulatory subunit alpha; PtdIns-3-kinase regulatory subunit p85-alpha Gene Symbols: Pik3r1 Molecular weight: 83,517 Da Basal Isoelectric point: 5.9  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 Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below PIK3R1 1A0N - A=91-104 (human) 1AZG - A=91-104 (human) 1H9O - A=617-724 (human) 1PBW - A/B=105-319 (human) 1PHT - A=1-85 (human) 1PIC - A=617-724 (human) 1PKS - A=1-79 (human) 1PKT - A=1-79 (human) 2IUG - A=321-440 (human) 2IUH - A=321-440 (human) 2IUI - A/B=321-440 (human) 2RD0 - B=322-600 (human) 2V1Y - B=431-600 (human) 3HHM - B=322-694 (human) 3HIZ - B=322-694 (human) 3I5R - A=1-83 (human) 3I5S - A/D/C/B=1-83 (human) 4A55 - B=322-600 (human) 1FU5 - A=322-431 (rat) 1FU6 - A=322-431 (rat) 1BFI - A=614-724 (cow) 1BFJ - A=614-724 (cow) 1OO3 - A=321-431 (cow) 1OO4 - A=321-431 (cow) 1PNJ - A=1-84 (cow) 1QAD - A=614-724 (cow) 2PNA - A=328-431 (cow) 2PNB - A=328-431 (cow) 2PNI - A=1-84 (cow)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  Source  |  UCSD-Nature A001772 A001773 A001775  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
signaling pathway regulation: S361‑p, S652‑p molecular association, regulation: S361‑p, S652‑p

	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.			mouse
0	1		Y59	DIGWLNGYNETTGER
0	1		Y73	RGDFPGTYVEYIGRK
0	3		Y76	FPGTYVEYIGRKRIS
3	1		S83	YIGRKRISPPTPKPR
1	0		T86	RKRISPPTPKPRPPR
0	1		S147	EKKGLECSTLYRTQs
0	1		T148	KKGLECSTLYRTQsS
0	1		T152	ECSTLYRTQsSSNPA
1	1		S154-p	STLYRTQsSSNPAEL
1	0		Y203	PVIPVAVYNEMMSLA
0	1		S265	LLNARVLSEIFSPVL
1	1		S361-p	TFLVRDAsTKMHGDY
2	3		Y368	sTKMHGDYTLTLRKG
0	1		T369	TKMHGDYTLTLRKGG
0	1		K382-u	GGNNKLIkIFHRDGK
0	1		Y416	RNESLAQYNPKLDVK
0	8		Y426-p	KLDVKLLyPVSKYQQ
0	450		Y452-p	VGKKLHEyNTQFQEK
0	3		T454	KKLHEyNTQFQEKSR
0	16		Y463	FQEKSREYDRLyEEy
8	2230		Y467-p	SREYDRLyEEyTRTS
0	42		Y470-p	YDRLyEEyTRTSQEI
0	5		Y504	QCQTQERYSKEyIEK
2	31		Y508-p	QERYSKEyIEKFKRE
1	8		H528	IQRIMHNHDKLKSRI
0	1		K530	RIMHNHDKLKSRISE
1	29		Y556	LKKQAAEYREIDKRM
0	15		T576-p	DLIQLRKtRDQyLMW
1	913		Y580-p	LRKtRDQyLMWLTQK
0	2		T603	EWLGNENTEDQysLV
1	253		Y607-p	NENTEDQysLVEDDE
3	24		S608-p	ENTEDQysLVEDDED
1	1		S652-p	TFLVRESsKQGCyAC
0	1		Y657-p	ESsKQGCyACSVVVD
0	15		Y679-p	INKTATGyGFAEPYN
3	0		Y688	FAEPYNLYSsLKELV
1	0		S690-p	EPYNLYSsLKELVLH

	human
Y59-p	EIGWLNGyNETTGER
Y73-p	RGDFPGTyVEyIGRK
Y76-p	FPGTyVEyIGRKKIs
S83-p	yIGRKKIsPPTPKPR
T86	RKKIsPPTPKPRPPR
S147-p	EKKGLECstLYRtQs
T148-p	KKGLECstLYRtQsS
T152-p	ECstLYRtQsSSNLA
S154-p	stLYRtQsSSNLAEL
Y203-p	PVIPAAVySEMISLA
S265-p	LLNARVLsEIFSPML
S361	TFLVRDASTKMHGDy
Y368-p	STKMHGDytLTLRKG
T369-p	TKMHGDytLTLRKGG
K382	GGNNKLIKIFHRDGK
Y416	RNESLAQYNPKLDVK
Y426-p	KLDVKLLyPVSKYQQ
Y452-p	VGKKLHEyNtQFQEK
T454-p	KKLHEyNtQFQEKSR
Y463-p	FQEKSREyDRLyEEy
Y467-p	SREyDRLyEEyTRTS
Y470-p	yDRLyEEyTRTSQEI
Y504-p	QCQTQERySKEyIEK
Y508-p	QERySKEyIEKFKRE
Y528-p	IQRIMHNyDkLKSRI
K530-a	RIMHNyDkLKSRISE
Y556-p	LKKQAAEyREIDKRM
T576-p	DLIQLRKtRDQyLMW
Y580-p	LRKtRDQyLMWLTQK
T603-p	EWLGNENtEDQysLV
Y607-p	NENtEDQysLVEDDE
S608-p	ENtEDQysLVEDDED
S652	TFLVRESSKQGCyAC
Y657-p	ESSKQGCyACSVVVD
Y679-p	INKTATGyGFAEPYN
Y688-p	FAEPYNLySSLKELV
S690	EPYNLySSLKELVLH

	rat
Y59	DIGWLNGYNETTGER
Y73	RGDFPGTYVEYIGRK
Y76	FPGTYVEYIGRKRIS
S83	YIGRKRISPPTPKPR
T86	RKRISPPTPKPRPPR
S147	EKKGLECSTLYRTQS
T148	KKGLECSTLYRTQSS
T152	ECSTLYRTQSSSNPA
S154	STLYRTQSSSNPAEL
Y203	PVIPVAVYNEMMSLA
S265	LLNARALSEIFSHVL
S361	TFLVRDASTKMHGDY
Y368	STKMHGDYTLTLRKG
T369	TKMHGDYTLTLRKGG
K382	GGNNKLIKIFHRDGK
Y416-p	RNESLAQyNPKLDVK
Y426-p	KLDVKLLyPVSKYQQ
Y452-p	VGKKLHEyNTQFQEK
T454	KKLHEyNTQFQEKSR
Y463	FQEKSREYDRLyEEy
Y467-p	SREYDRLyEEyTRTS
Y470-p	YDRLyEEyTRTSQEI
Y504	QCHPQERYSKDyIEK
Y508-p	QERYSKDyIEKFKRE
H528	IQRIMHNHDKLKSRI
K530	RIMHNHDKLKSRISE
Y556	LKKQAAEYREIDKRM
T576	DLIQLRKTRDQyLMW
Y580-p	LRKTRDQyLMWLTQK
T603	EWLGNENTEDQYsLV
Y607	NENTEDQYsLVDDDE
S608-p	ENTEDQYsLVDDDED
S652	TFLVRESSKQGCYAC
Y657	ESSKQGCYACSVVVD
Y679	INKTATGYGFAEPYN
Y688	FAEPYNLYSSLKELV
S690	EPYNLYSSLKELVLH

	cow
Y59	EIGWLNGYNETTGER
Y73	RGDFPGTYVEYIGRK
Y76	FPGTYVEYIGRKKIs
S83-p	YIGRKKIsPPtPKPR
T86-p	RKKIsPPtPKPRPPR
S147	EKKGLECSTLYRTQS
T148	KKGLECSTLYRTQSS
T152	ECSTLYRTQSSSNPA
S154	STLYRTQSSSNPAEL
S203	PVIPVAVSSELISLA
S265	LLNARVLSELFSPLL
S361	TFLVRDASTKMHGDy
Y368-p	STKMHGDyTLTLRKG
T369	TKMHGDyTLTLRKGG
K382	GGNNKLIKIFHRDGK
Y416	RNESLAQYNPKLDVK
Y426	KLDVKLLYPVSKYQQ
Y452	VGKKLHEYNTQFQEK
T454	KKLHEYNTQFQEKSR
Y463	FQEKSREYDRLYEDY
Y467	SREYDRLYEDYTRTS
Y470	YDRLYEDYTRTSQEI
Y504	QCQTQERYSKEYIEK
Y508	QERYSKEYIEKFKRE
Y528	IQRIMHNYEKLKSRI
K530	RIMHNYEKLKSRISE
Y556	LKKQAAEYREIDKRM
T576	DLIQLRKTRDQYLMW
Y580	LRKTRDQYLMWLTQK
T603	EWLGNENTEDQYsLV
Y607	NENTEDQYsLVEDDE
S608-p	ENTEDQYsLVEDDED
S652	TFLVRESSKQGCYAC
Y657	ESSKQGCYACSVVVD
Y679	INKTATGYGFAEPYN
Y688-p	FAEPYNLySSLKELV
S690	EPYNLySSLKELVLH

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