Home

PIK3R3 (human)

Overview PIK3R3 Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1. Heterodimer of a regulatory subunit PIK3R3 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with AXL. Highest levels in brain and testis. Lower levels in adipose tissue, kidney, heart, lung and skeletal muscle. Belongs to the PI3K p85 subunit family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB. Protein type: Kinase, lipid; Motility/polarity/chemotaxis Cellular Component: phosphoinositide 3-kinase complex; cytosol Molecular Function: 1-phosphatidylinositol-3-kinase activity; 1-phosphatidylinositol-3-kinase regulator activity Biological Process: platelet activation; phospholipid metabolic process; T cell costimulation; insulin receptor signaling pathway; phosphatidylinositol biosynthetic process; blood coagulation Reference #:  Q92569 (UniProtKB) Alt. Names/Synonyms: 100% homology to SWISS-PROT Q92569; DKFZp686P05226; FLJ41892; p55; p55-GAMMA; P55G; p55PIK; Phosphatidylinositol 3-kinase 55 kDa regulatory subunit gamma; Phosphatidylinositol 3-kinase regulatory subunit gamma; phosphatidylinositol 3-kinase, regulatory subunit, polypeptide 3 (p55, gamma); phosphoinositide-3-kinase, regulatory subunit 3 (gamma); phosphoinositide-3-kinase, regulatory subunit 3 (p55, gamma); phosphoinositide-3-kinase, regulatory subunit, polypeptide 3 (p55, gamma); PI3-kinase regulatory subunit gamma; PI3-kinase subunit p55-gamma; PI3K regulatory subunit gamma; PIK3R3; PtdIns-3-kinase regulatory subunit gamma; PtdIns-3-kinase regulatory subunit p55-gamma Gene Symbols: PIK3R3 Molecular weight: 54,448 Da Basal Isoelectric point: 5.68  Predict pI for various phosphorylation states CST Pathways:  Adherens Junction Dynamics  |  AMPK Signaling  |  Angiogenesis  |  Apoptosis  |  ErbB/HER Signaling  |  ESC Pluripotency and Differentiation  |  Inhibition of Apoptosis  |  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 PIK3R3

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  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		K106-a	DYTLTLRkGGNNKLI
0	1		K114-a	GGNNKLIkIYHRDGK
0	1		Y158	KLDVKLMYPVSRYQQ
0	18		Y184-p	VGKKLQEyHsQyQEK
0	5		S186-p	KKLQEyHsQyQEKSK
0	9		Y188-p	LQEyHsQyQEKSKEy
0	5		Y195-p	yQEKSKEyDRLyEEy
2	704		Y199-p	SKEyDRLyEEytRTS
0	39		Y202-p	yDRLyEEytRTSQEI
0	16		T203-p	DRLyEEytRTSQEIQ
0	3		Y260-p	IERIMMNyDKLKSRL
1	34		Y341-p	NEDADENyFINEEDE
0	2		Y373-p	VQAEDLLyGKPDGAF
0	11		Y407-p	EVKHCVIySTARGYG

	mouse
K106	DYTLTLRKGGNNKLI
K114	GGNNKLIKIYHRDGK
Y158-p	KLDVKLTyPVSRFQQ
F184	VGKNLQEFHSQYQEK
S186	KNLQEFHSQYQEKSK
Y188	LQEFHSQYQEKSKEY
Y195	YQEKSKEYDRLyEEy
Y199-p	SKEYDRLyEEytRTS
Y202-p	YDRLyEEytRTSQEI
T203-p	DRLyEEytRTSQEIQ
Y260	IERIMMNYDKLKSRL
Y341-p	NEDSDESyFINEEDE
Y373	VQAEDLLYGKPDGAF
Y407	EVKHCVIYSTARGYG

	rat
K106	DYTLTLRKGGNNKLI
K114	GGNNKLIKIYHRDGN
Y158	KLDVKLMYPVSRYQQ
F184	VGKNLQEFHSQYQEK
S186	KNLQEFHSQYQEKSK
Y188	LQEFHSQYQEKSKEY
Y195	YQEKSKEYDRLyEEY
Y199-p	SKEYDRLyEEYTRTS
Y202	YDRLyEEYTRTSQEI
T203	DRLyEEYTRTSQEIQ
Y260	IERIMMNYDKLKSRL
Y341	SEDTDESYFINEDDE
Y373	VQAEDLLYGKPDGAF
Y407	EVKPCVIYSPARGYG

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.