PIK3R1

From Wikipedia, the free encyclopedia

Phosphoinositide-3-kinase, regulatory subunit 1 (p85 alpha)

PDB rendering based on 1bfi.

Available structures: 1bfi, 1bfj, 1fu5, 1fu6, 1h9o, 1oo3, 1oo4, 1pbw, 1pht, 1pic, 1pks, 1pkt, 1pnj, 1qad, 2iug, 2iuh, 2iui, 2pna, 2pnb, 2pni

Identifiers

Symbol(s)

PIK3R1; GRB1; p85-ALPHA

External IDs

OMIM: 171833 HomoloGene: 7889

Gene ontology
Molecular Function:	• insulin receptor binding • insulin-like growth factor receptor binding • phosphatidylinositol binding • protein phosphatase binding • phosphoinositide 3-kinase regulator activity • ErbB-3 class receptor binding • insulin binding • insulin receptor substrate binding
Cellular Component:	• intracellular • cytoplasm • cytosol • membrane • phosphoinositide 3-kinase complex, class IA
Biological Process:	• protein amino acid phosphorylation • intracellular signaling cascade • insulin receptor signaling pathway • B cell differentiation • negative regulation of apoptosis • phosphoinositide phosphorylation • insulin-like growth factor receptor signaling pathway

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

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Refseq

NM_181504 (mRNA)
NP_852556 (protein)

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Location

Chr 5: 67.55 - 67.63 Mb

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Pubmed search

[1]

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Phosphoinositide-3-kinase, regulatory subunit 1 (p85 alpha), also known as PIK3R1, is a human gene.

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.^[1]

[edit] References

^ Entrez Gene: PIK3R1 phosphoinositide-3-kinase, regulatory subunit 1 (p85 alpha).

[edit] 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. 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, et al. (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. 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, et al. (2004). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication.". J. Biosci. 28 (3): 323–35. PMID 12734410.
Leavitt SA, SchOn A, Klein JC, et al. (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. PMID 14965316.
Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection.". Curr. HIV Res. 3 (1): 87–94. PMID 15638726.