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PIK3R1 (human)

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; Enzyme, regulatory subunit; Kinase, lipid Cellular Component: plasma membrane; cytosol; phosphoinositide 3-kinase complex; nucleus Molecular Function: protein C-terminus binding; protein domain specific binding; neurotrophin TRKA receptor binding; 1-phosphatidylinositol-3-kinase activity; phosphoprotein binding; 1-phosphatidylinositol-3-kinase regulator activity; phosphoinositide 3-kinase regulator activity; protein kinase binding; transmembrane receptor protein tyrosine kinase adaptor protein activity; protein phosphatase binding; ATPase binding; insulin receptor binding; calmodulin binding; insulin binding; insulin-like growth factor receptor binding; protein binding; ErbB-3 class receptor binding; ubiquitin protein ligase binding; insulin receptor substrate binding; phosphoinositide 3-kinase binding; estrogen receptor binding; phosphatidylinositol binding Biological Process: negative regulation of osteoclast differentiation; phosphoinositide 3-kinase cascade; response to cAMP; negative regulation of heart rate; nerve growth factor receptor signaling pathway; negative regulation of smooth muscle cell proliferation; positive regulation of apoptosis; protein amino acid phosphorylation; T cell receptor signaling pathway; NFAT protein import into nucleus; regulation of phosphoinositide 3-kinase activity; response to estradiol stimulus; positive regulation of glucose import; phosphoinositide phosphorylation; phospholipid metabolic process; response to yeast; negative regulation of blood pressure; response to iron(II) ion; response to nutrient; response to fructose stimulus; response to drug; negative regulation of proteolysis; epidermal growth factor receptor signaling pathway; platelet activation; fibroblast growth factor receptor signaling pathway; phosphoinositide-mediated signaling; glucose metabolic process; response to testosterone stimulus; negative regulation of cell-matrix adhesion; response to amino acid stimulus; positive regulation of myoblast differentiation; response to ethanol; insulin-like growth factor receptor signaling pathway; virus-host interaction; B cell differentiation; T cell costimulation; phosphatidylinositol biosynthetic process; 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; blood coagulation; response to progesterone stimulus; leukocyte migration; positive regulation of cell migration; negative regulation of apoptosis Reference #:  P27986 (UniProtKB) Alt. Names/Synonyms: GRB1; p85; p85-ALPHA; P85A; Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha; Phosphatidylinositol 3-kinase regulatory subunit alpha; phosphatidylinositol 3-kinase, regulatory subunit, polypeptide 1 (p85 alpha); phosphatidylinositol 3-kinase, regulatory, 1; phosphatidylinositol 3-kinase-associated p-85 alpha; phosphoinositide-3-kinase, regulatory subunit 1 (alpha); PI3-kinase regulatory subunit alpha; PI3-kinase subunit p85-alpha; PI3K regulatory subunit alpha; PIK3R1; PtdIns-3-kinase regulatory subunit alpha; PtdIns-3-kinase regulatory subunit p85-alpha Gene Symbols: PIK3R1 Molecular weight: 83,598 Da Basal Isoelectric point: 5.84  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  |  RCSB PDB 1A0N 1AZG 1H9O 1PBW 1PHT 1PIC 1PKS 1PKT 2IUG 2IUH 2IUI 2RD0 2V1Y 3HHM 3HIZ 3I5R 3I5S 4A55  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature A001772 A001773 A001775  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
cell motility, altered: Y528‑p, Y556‑p activation: S608‑p enzymatic activity, induced: Y528‑p, Y556‑p molecular association, regulation: Y528‑p, Y556‑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.			human
0	1		Y59-p	EIGWLNGyNETTGER
0	1		Y73-p	RGDFPGTyVEyIGRK
0	3		Y76-p	FPGTyVEyIGRKKIs
3	1		S83-p	yIGRKKIsPPTPKPR
1	0		T86	RKKIsPPTPKPRPPR
0	1		S147-p	EKKGLECstLYRtQs
0	1		T148-p	KKGLECstLYRtQsS
0	1		T152-p	ECstLYRtQsSSNLA
1	1		S154-p	stLYRtQsSSNLAEL
1	0		Y203-p	PVIPAAVySEMISLA
0	1		S265-p	LLNARVLsEIFSPML
1	1		S361	TFLVRDASTKMHGDy
2	3		Y368-p	STKMHGDytLTLRKG
0	1		T369-p	TKMHGDytLTLRKGG
0	1		K382	GGNNKLIKIFHRDGK
0	1		Y416	RNESLAQYNPKLDVK
0	8		Y426-p	KLDVKLLyPVSKYQQ
0	450		Y452-p	VGKKLHEyNtQFQEK
0	3		T454-p	KKLHEyNtQFQEKSR
0	16		Y463-p	FQEKSREyDRLyEEy
8	2230		Y467-p	SREyDRLyEEyTRTS
0	42		Y470-p	yDRLyEEyTRTSQEI
0	5		Y504-p	QCQTQERySKEyIEK
2	31		Y508-p	QERySKEyIEKFKRE
1	8		Y528-p	IQRIMHNyDkLKSRI
0	1		K530-a	RIMHNyDkLKSRISE
1	29		Y556-p	LKKQAAEyREIDKRM
0	15		T576-p	DLIQLRKtRDQyLMW
1	913		Y580-p	LRKtRDQyLMWLTQK
0	2		T603-p	EWLGNENtEDQysLV
1	253		Y607-p	NENtEDQysLVEDDE
3	24		S608-p	ENtEDQysLVEDDED
1	1		S652	TFLVRESSKQGCyAC
0	1		Y657-p	ESSKQGCyACSVVVD
0	15		Y679-p	INKTATGyGFAEPYN
3	0		Y688-p	FAEPYNLySSLKELV
1	0		S690	EPYNLySSLKELVLH

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