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PIK3R1

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PIK3R1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPIK3R1, AGM7, GRB1, IMD36, p85, p85-ALPHA, phosphoinositide-3-kinase regulatory subunit 1, PI3KR1
External IDsOMIM: 171833; MGI: 97583; HomoloGene: 7889; GeneCards: PIK3R1; OMA:PIK3R1 - orthologs
Orthologs
SpeciesHumanMouse
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 MbChr 13: 101.82 – 101.9 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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 Template:SWL.[7]

Mutations in PIK3R1 are associated to Template:SWL.[8]

Interactions

PIK3R1 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000145675 – Ensembl, May 2017
  2. ^ a b c 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.
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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.
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