ITPKA

From Wikipedia, the free encyclopedia

Inositol 1,4,5-trisphosphate 3-kinase A

PDB rendering based on 1tzd.

Available structures: 1tzd, 1w2c, 1w2d, 1w2f

Identifiers

Symbol(s)

ITPKA;

External IDs

OMIM: 147521 MGI: 1333822 HomoloGene: 1671

Gene ontology
Molecular Function:	• nucleotide binding • calmodulin binding • ATP binding • inositol trisphosphate 3-kinase activity • kinase activity • transferase activity
Biological Process:	• inositol metabolic process • signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002220 (mRNA)
NP_002211 (protein)

XM_001003136 (mRNA)
XP_001003136 (protein)

Location

Chr 15: 39.57 - 39.58 Mb

Chr 2: 119.43 - 119.44 Mb

Pubmed search

[1]

[2]

Inositol 1,4,5-trisphosphate 3-kinase A, also known as ITPKA, is a human gene.^[1]

Regulates inositol phosphate metabolism by phosphorylation of second messenger inositol 1,4,5-trisphosphate to Ins(1,3,4,5)P4. The activity of the inositol 1,4,5-trisphosphate 3-kinase is responsible for regulating the levels of a large number of inositol polyphosphates that are important in cellular signaling. Both calcium/calmodulin and protein phosphorylation mechanisms control its activity. It is also a substrate for the cyclic AMP-dependent protein kinase, calcium/calmodulin- dependent protein kinase II, and protein kinase C in vitro. ITPKA and ITPKB are 68% identical in the C-terminus region.^[1]

[edit] References

^ ^a ^b Entrez Gene: ITPKA inositol 1,4,5-trisphosphate 3-kinase A.

[edit] Further reading

Erneux C, Roeckel N, Takazawa K, et al. (1992). "Localization of the genes for human inositol 1,4,5-trisphosphate 3-kinase A (ITPKA) and B (ITPKB) to chromosome regions 15q14-q21 and 1q41-q43, respectively, by in situ hybridization.". Genomics 14 (2): 546-7. PMID 1330886.
Takazawa K, Perret J, Dumont JE, Erneux C (1991). "Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme.". Biochem. J. 278 ( Pt 3): 883-6. PMID 1654894.
Takazawa K, Erneux C (1992). "Identification of residues essential for catalysis and binding of calmodulin in rat brain inositol 1,4,5-trisphosphate 3-kinase.". Biochem. J. 280 ( Pt 1): 125-9. PMID 1660262.
Takazawa K, Perret J, Dumont JE, Erneux C (1991). "Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase.". Biochem. Biophys. Res. Commun. 174 (2): 529-35. PMID 1847047.
Lin AN, Barnes S, Wallace RW (1990). "Phosphorylation by protein kinase C inactivates an inositol 1,4,5-trisphosphate 3-kinase purified from human platelets.". Biochem. Biophys. Res. Commun. 170 (3): 1371-6. PMID 2167676.
Takazawa K, Perret J, Dumont JE, Erneux C (1991). "Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence.". Nucleic Acids Res. 18 (23): 7141. PMID 2175886.
Takazawa K, Vandekerckhove J, Dumont JE, Erneux C (1991). "Cloning and expression in Escherichia coli of a rat brain cDNA encoding a Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase.". Biochem. J. 272 (1): 107-12. PMID 2176078.
Ryu SH, Lee SY, Lee KY, Rhee SG (1987). "Catalytic properties of inositol trisphosphate kinase: activation by Ca2+ and calmodulin.". FASEB J. 1 (5): 388-93. PMID 2824270.
Communi D, Vanweyenberg V, Erneux C (1997). "D-myo-inositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calcium:calmodulin-dependent protein kinase II phosphorylation mechanism.". EMBO J. 16 (8): 1943-52. doi:10.1093/emboj/16.8.1943. PMID 9155020.
Woodring PJ, Garrison JC (1997). "Expression, purification, and regulation of two isoforms of the inositol 1,4,5-trisphosphate 3-kinase.". J. Biol. Chem. 272 (48): 30447-54. PMID 9374536.
Schell MJ, Erneux C, Irvine RF (2001). "Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus.". J. Biol. Chem. 276 (40): 37537-46. doi:10.1074/jbc.M104101200. PMID 11468283.
Mishra J, Bhalla US (2003). "Simulations of inositol phosphate metabolism and its interaction with InsP(3)-mediated calcium release.". Biophys. J. 83 (3): 1298-316. PMID 12202356.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Dewaste V, Moreau C, De Smedt F, et al. (2003). "The three isoenzymes of human inositol-1,4,5-trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in COS-7 cells.". Biochem. J. 374 (Pt 1): 41-9. doi:10.1042/BJ20021963. PMID 12747803.
González B, Schell MJ, Letcher AJ, et al. (2004). "Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase.". Mol. Cell 15 (5): 689-701. doi:10.1016/j.molcel.2004.08.004. PMID 15350214.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Kato H, Uzawa K, Onda T, et al. (2006). "Down-regulation of 1D-myo-inositol 1,4,5-trisphosphate 3-kinase A protein expression in oral squamous cell carcinoma.". Int. J. Oncol. 28 (4): 873-81. PMID 16525636.