PIK3R1

Phosphatidylinositol 3-kinase regulatory subunit alpha is an enzyme that in humans is encoded by the PIK3R1 gene.[5]

PIK3R1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1A0N, 1AZG, 1H9O, 1PBW, 1PHT, 1PIC, 1PKS, 1PKT, 2IUG, 2IUH, 2IUI, 2RD0, 2V1Y, 3HHM, 3HIZ, 3I5R, 3I5S, 4A55, 4JPS, 4L1B, 4L23, 4L2Y, 4OVU, 4OVV, 4WAF, 5AUL
Identifiers
Aliases	PIK3R1, AGM7, GRB1, IMD36, p85, p85-ALPHA, phosphoinositide-3-kinase regulatory subunit 1, PI3KR1
External IDs	OMIM: 171833 MGI: 97583 HomoloGene: 7889 GeneCards: PIK3R1
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q13.1 Start 68,215,756 bp[1] End 68,301,821 bp[1]
Gene location (Mouse) Chr. Chromosome 13 (mouse)[2] Band 13 D1|13 53.92 cM Start 101,680,563 bp[2] End 101,768,217 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • ErbB-3 class receptor binding • phosphatidylinositol 3-kinase regulator activity • insulin-like growth factor receptor binding • transmembrane receptor protein tyrosine kinase adaptor activity • insulin receptor binding • neurotrophin TRKA receptor binding • phosphatidylinositol 3-kinase regulatory subunit binding • transcription factor binding • insulin binding • phosphatidylinositol 3-kinase binding • 1-phosphatidylinositol-3-kinase regulator activity • GO:0001948 protein binding • protein heterodimerization activity • insulin receptor substrate binding • protein phosphatase binding • 1-phosphatidylinositol-3-kinase activity • phosphatidylinositol-4,5-bisphosphate 3-kinase activity • phosphotyrosine residue binding Cellular component • cytoplasm • cytosol • phosphatidylinositol 3-kinase complex • phosphatidylinositol 3-kinase complex, class IA • membrane • intercellular junction • cis-Golgi network • cell membrane • cell nucleus • perinuclear endoplasmic reticulum membrane • macromolecular complex Biological process • positive regulation of glucose import • insulin-like growth factor receptor signaling pathway • negative regulation of cell adhesion • positive regulation of endoplasmic reticulum unfolded protein response • epidermal growth factor receptor signaling pathway • Fc-gamma receptor signaling pathway involved in phagocytosis • negative regulation of osteoclast differentiation • positive regulation of cell migration • cellular glucose homeostasis • cellular response to UV • T cell costimulation • protein stabilization • negative regulation of apoptotic process • response to endoplasmic reticulum stress • regulation of stress fiber assembly • negative regulation of cell-matrix adhesion • platelet activation • Fc-epsilon receptor signaling pathway • protein phosphorylation • phosphatidylinositol phosphorylation • vascular endothelial growth factor receptor signaling pathway • growth hormone receptor signaling pathway • regulation of phosphatidylinositol 3-kinase activity • intrinsic apoptotic signaling pathway in response to DNA damage • cellular response to insulin stimulus • positive regulation of tumor necrosis factor production • positive regulation of RNA splicing • phosphatidylinositol biosynthetic process • protein transport • B cell differentiation • GO:0022415 viral process • T cell receptor signaling pathway • extrinsic apoptotic signaling pathway via death domain receptors • phosphatidylinositol-mediated signaling • leukocyte migration • positive regulation of transcription from RNA polymerase II promoter • signal transduction • phosphatidylinositol 3-kinase signaling • phosphatidylinositol-3-phosphate biosynthetic process • ERBB2 signaling pathway • insulin receptor signaling pathway • axon guidance • regulation of insulin receptor signaling pathway • interleukin-7-mediated signaling pathway • transport • regulation of protein localization to plasma membrane • positive regulation of protein localization to plasma membrane • G-protein coupled receptor signaling pathway • positive regulation of protein kinase B signaling • protein import into nucleus • positive regulation of phosphatidylinositol 3-kinase signaling • cytokine-mediated signaling pathway • positive regulation of protein import into nucleus Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5295	18708
Ensembl	ENSG00000145675	ENSMUSG00000041417
UniProt	P27986	P26450
RefSeq (mRNA)	NM_001242466 NM_181504 NM_181523 NM_181524	NM_001024955 NM_001077495
RefSeq (protein)	NP_001229395 NP_852556 NP_852664 NP_852665	NP_001020126 NP_001070963
Location (UCSC)	Chr 5: 68.22 – 68.3 Mb	Chr 13: 101.68 – 101.77 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Phosphatidylinositol 3-kinase phosphorylates the inositol ring of phosphatidylinositol at the 3-prime position. The enzyme comprises a 110 kD catalytic subunit and a regulatory subunit of either 85, 55, or 50 kD. This gene encodes the 85 kD regulatory subunit. Phosphatidylinositol 3-kinase plays an important role in the metabolic actions of insulin, and a mutation in this gene has been associated with insulin resistance. Alternative splicing of this gene results in three transcript variants encoding different isoforms.[6]

Clinical significance

Mutations in PIK3R1 are implicated in cases of breast cancer.[7]

Mutations in PIK3R1 are associated to SHORT syndrome.[8]

Interactions

PIK3R1 has been shown to interact with:

• ADAM12,[9]
• BCAR1,[10]
• CBLB,[11][12]
• CD117,[13][14][15]
• CD28,[16]
• CD7,[17][18]
• CENTG1,[19]
• CBL,[20][21][22]
• EPHA2,[23]
• EPOR,[24][25]
• ERBB3,[26][27]
• EZR,[28]
• FCGR2A,[29][30]
• GAB1,[31][32][33]
• GAB2,[34][35]
• Grb2,[36][37]
• HRAS,[38][39]
• IRS1[40][41][42][43]
• IRS2,[40][44][45][46]
• IL1R1,[47]
• JAK2,[48]
• KHDRBS1,[49][50]
• LTK,[51][52]
• LAT,[53]
• LCP2,[54]
• PIK3CD,[55]
• PTK2,[56]
• SHB,[57]
• TUBA1B,[58]
• TYRO3,[59]
• VAV1,[24][31] and
• WAS.[60]

References

1. GRCh38: Ensembl release 89: ENSG00000145675 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000041417 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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6. "Entrez Gene: PIK3R1 phosphoinositide-3-kinase, regulatory subunit 1 (p85 alpha)".
7. The Cancer Genome Atlas Network (October 2012). "Comprehensive molecular portraits of human breast tumours". Nature. 490 (7418): 61–70. doi:10.1038/nature11412. PMC 3465532. PMID 23000897.
8. Bárcena C, Quesada V, De Sandre-Giovannoli A, Puente DA, Fernández-Toral J, Sigaudy S, Baban A, Lévy N, Velasco G, López-Otín C (2014). "Exome sequencing identifies a novel mutation in PIK3R1 as the cause of SHORT syndrome". BMC Med. Genet. 15 (1): 51. doi:10.1186/1471-2350-15-51. PMC 4022398. PMID 24886349.
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Further reading

• Benito M, Valverde AM, Lorenzo M (1996). "IGF-I: a mitogen also involved in differentiation processes in mammalian cells". Int. J. Biochem. Cell Biol. 28 (5): 499–510. doi:10.1016/1357-2725(95)00168-9. PMID 8697095.
• Snapper SB, Rosen FS (1999). "The Wiskott-Aldrich syndrome protein (WASP): roles in signaling and cytoskeletal organization". Annu. Rev. Immunol. 17: 905–29. doi:10.1146/annurev.immunol.17.1.905. PMID 10358777.
• Katada T, Kurosu H, Okada T, Suzuki T, Tsujimoto N, Takasuga S, Kontani K, Hazeki O, Ui M (1999). "Synergistic activation of a family of phosphoinositide 3-kinase via G-protein coupled and tyrosine kinase-related receptors". Chem. Phys. Lipids. 98 (1–2): 79–86. doi:10.1016/S0009-3084(99)00020-1. PMID 10358930.
• Zhang W, Samelson LE (2000). "The role of membrane-associated adaptors in T cell receptor signalling". Semin. Immunol. 12 (1): 35–41. doi:10.1006/smim.2000.0205. PMID 10723796.
• Greenway AL, Holloway G, McPhee DA, Ellis P, Cornall A, Lidman M (2003). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication". J. Biosci. 28 (3): 323–35. doi:10.1007/BF02970151. PMID 12734410.
• Leavitt SA, SchOn A, Klein JC, Manjappara U, Chaiken IM, Freire E (2004). "Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm". Curr. Protein Pept. Sci. 5 (1): 1–8. doi:10.2174/1389203043486955. PMID 14965316.
• Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection". Curr. HIV Res. 3 (1): 87–94. doi:10.2174/1570162052773013. PMID 15638726.