Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
PIK3R1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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: Kinase, lipid; Motility/polarity/chemotaxis; Enzyme, regulatory subunit
Cellular Component: plasma membrane; phosphoinositide 3-kinase complex; cytosol
Molecular Function: insulin binding; insulin-like growth factor receptor binding; protein binding; ErbB-3 class receptor binding; neurotrophin TRKA receptor binding; insulin receptor substrate binding; phosphoinositide 3-kinase binding; phosphoinositide 3-kinase regulator activity; transmembrane receptor protein tyrosine kinase adaptor protein activity; protein phosphatase binding; insulin receptor binding
Biological Process: negative regulation of osteoclast differentiation; phosphoinositide 3-kinase cascade; nerve growth factor receptor signaling pathway; viral reproduction; regulation of phosphoinositide 3-kinase activity; T cell receptor signaling pathway; NFAT protein import into nucleus; protein amino acid phosphorylation; positive regulation of glucose import; phosphoinositide phosphorylation; phospholipid metabolic process; epidermal growth factor receptor signaling pathway; platelet activation; phosphoinositide-mediated signaling; fibroblast growth factor receptor signaling pathway; negative regulation of cell-matrix adhesion; positive regulation of tumor necrosis factor production; induction of apoptosis via death domain receptors; DNA damage response, signal transduction resulting in induction of apoptosis; insulin-like growth factor receptor signaling pathway; B cell differentiation; T cell costimulation; phosphatidylinositol biosynthetic process; insulin receptor signaling pathway; innate immune response; positive regulation of transcription from RNA polymerase II promoter; blood coagulation; leukocyte migration; negative regulation of apoptosis; positive regulation of cell migration
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:  Actin Dynamics  |  Adherens Junction Dynamics  |  AMPK Signaling  |  Angiogenesis  |  Apoptosis Regulation  |  B Cell Receptor Signaling  |  ErbB/HER Signaling  |  ESC Pluripotency and Differentiation  |  Growth And Differentiation Control by MAPKs  |  IL6 Signaling  |  Inhibition of Apoptosis  |  Insulin Receptor Signaling  |  Microtubule Dynamics  |  Mitochondrial Control of Apoptosis  |  mTOR Signaling  |  NF-kB Signaling  |  PI3K/Akt Signaling  |  Protein Kinase C Signaling  |  SAPK/JNK Signaling Cascades  |  T Cell Receptor Signaling  |  TGF-├č Signaling  |  Translation: eIF4E and p70S6K  |  Warburg Effect
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PIK3R1

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
cell motility, altered: Y528‑p, Y556‑p
activity, induced: 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
 

Show Multiple Sequence Alignment


 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 3 Y76-p FPGTYVEyIGRKKIs
3 1 S83-p yIGRKKIsPPTPKPR
1 0 T86 RKKIsPPTPKPRPPR
1 2 S154-p STLYRTQsSSNLAEL
1 0 Y203-p PVIPAAVySEMISLA
0 1 S265-p LLNARVLsEIFSPML
0 1 S279-p LFRFSAAsSDNTENL
1 1 S361 TFLVRDASTKMHGDy
2 2 Y368-p STKMHGDyTLTLRKG
0 1 K382 GGNNKLIKIFHRDGK
0 8 Y426-p KLDVKLLyPVSKYQQ
0 450 Y452-p VGKKLHEyNtQFQEK
0 3 T454-p KKLHEyNtQFQEKSR
0 16 Y463-p FQEKSREyDRLyEEy
8 2232 Y467-p SREyDRLyEEyTRTS
0 42 Y470-p yDRLyEEyTRTSQEI
0 5 Y504-p QCQTQERySKEyIEK
2 32 Y508-p QERySKEyIEKFKRE
1 8 Y528-p IQRIMHNyDkLKSRI
0 1 K530-a RIMHNyDkLKSRISE
1 29 Y556-p LKKQAAEyREIDKRM
0 15 T576-p DLIQLRKtRDQyLMW
1 915 Y580-p LRKtRDQyLMWLTQK
0 2 T603-p EWLGNENtEDQysLV
1 254 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
4228 : Phospho-PI3K p85 (Tyr458)/p55 (Tyr199) Antibody
  mouse

 
Y76 FPGTYVEYIGRKRIS
S83 YIGRKRISPPTPKPR
T86 RKRISPPTPKPRPPR
S154-p STLYRTQsSSNPAEL
Y203 PVIPVAVYNEMMSLA
S265 LLNARVLSEIFSPVL
S279 LFRFPAASSDNTEHL
S361-p TFLVRDAsTKMHGDY
Y368 sTKMHGDYTLTLRKG
K382-u GGNNKLIkIFHRDGK
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
4228 : Phospho-PI3K p85 (Tyr458)/p55 (Tyr199) Antibody
  rat

 
Y76 FPGTYVEYIGRKRIS
S83 YIGRKRISPPTPKPR
T86 RKRISPPTPKPRPPR
S154 STLYRTQSSSNPAEL
Y203 PVIPVAVYNEMMSLA
S265 LLNARALSEIFSHVL
S279 LFRFPAASSDNTEHL
S361 TFLVRDASTKMHGDY
Y368 STKMHGDYTLTLRKG
K382 GGNNKLIKIFHRDGK
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
4228 : Phospho-PI3K p85 (Tyr458)/p55 (Tyr199) Antibody
  cow

 
Y76 FPGTYVEYIGRKKIs
S83-p YIGRKKIsPPtPKPR
T86-p RKKIsPPtPKPRPPR
S154 STLYRTQSSSNPAEL
S203 PVIPVAVSSELISLA
S265 LLNARVLSELFSPLL
S279 LFRFPAASSENTEHL
S361 TFLVRDASTKMHGDy
Y368-p STKMHGDyTLTLRKG
K382 GGNNKLIKIFHRDGK
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
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.