ITPKA: Difference between revisions

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{{Infobox_gene}}
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'''Inositol-trisphosphate 3-kinase A''' is an [[enzyme]] that in humans is encoded by the ''ITPKA'' [[gene]].<ref name="pmid1330886">{{cite journal |vauthors=Erneux C, Roeckel N, Takazawa K, Mailleux P, Vassart G, Mattei MG | title = 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 | journal = Genomics | volume = 14 | issue = 2 | pages = 546–7 |date=Dec 1992 | pmid = 1330886 | pmc =  | doi =10.1016/S0888-7543(05)80265-4 }}</ref><ref name="pmid2175886">{{cite journal |vauthors=Takazawa K, Perret J, Dumont JE, Erneux C | title = Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence | journal = Nucleic Acids Res | volume = 18 | issue = 23 | pages = 7141 |date=Feb 1991 | pmid = 2175886 | pmc = 332787 | doi =10.1093/nar/18.23.7141 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ITPKA inositol 1,4,5-trisphosphate 3-kinase A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3706| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_ITPKA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1tzd.
| PDB = {{PDB2|1tzd}}, {{PDB2|1w2c}}, {{PDB2|1w2d}}, {{PDB2|1w2f}}
| Name = Inositol 1,4,5-trisphosphate 3-kinase A
| HGNCid = 6178
| Symbol = ITPKA
| AltSymbols =;
| OMIM = 147521
| ECnumber =
| Homologene = 1671
| MGIid = 1333822
  | GeneAtlas_image1 = PBB_GE_ITPKA_205874_at_tn.png
  | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008440 |text = inositol trisphosphate 3-kinase activity}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =  
| Process = {{GNF_GO|id=GO:0006020 |text = inositol metabolic process}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3706
    | Hs_Ensembl = ENSG00000137825
    | Hs_RefseqProtein = NP_002211
    | Hs_RefseqmRNA = NM_002220
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 39573365
    | Hs_GenLoc_end = 39583035
    | Hs_Uniprot = P23677
    | Mm_EntrezGene = 228550
    | Mm_Ensembl = ENSMUSG00000027296
    | Mm_RefseqmRNA = XM_001003136
    | Mm_RefseqProtein = XP_001003136
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 119433778
    | Mm_GenLoc_end = 119442694
    | Mm_Uniprot = Q8R071
  }}
}}
'''Inositol 1,4,5-trisphosphate 3-kinase A''', also known as '''ITPKA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ITPKA inositol 1,4,5-trisphosphate 3-kinase A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3706| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: ITPKA inositol 1,4,5-trisphosphate 3-kinase A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3706| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Erneux C, Roeckel N, Takazawa K, ''et al.'' |title=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. |journal=Genomics |volume=14 |issue= 2 |pages= 546-7 |year= 1992 |pmid= 1330886 |doi=  }}
*{{cite journal  |vauthors=Takazawa K, Perret J, Dumont JE, Erneux C |title=Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme |journal=Biochem. J. |volume=278 ( Pt 3) |issue= Pt 3|pages= 883–6 |year= 1991 |pmid= 1654894 |doi= | pmc=1151429 }}
*{{cite journal  | author=Takazawa K, Perret J, Dumont JE, Erneux C |title=Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme. |journal=Biochem. J. |volume=278 ( Pt 3) |issue=  |pages= 883-6 |year= 1991 |pmid= 1654894 |doi=  }}
*{{cite journal  |vauthors=Takazawa K, Erneux C |title=Identification of residues essential for catalysis and binding of calmodulin in rat brain inositol 1,4,5-trisphosphate 3-kinase |journal=Biochem. J. |volume=280 ( Pt 1) |issue=  Pt 1|pages= 125–9 |year= 1992 |pmid= 1660262 |doi=  | pmc=1130609  }}
*{{cite journal  | author=Takazawa K, Erneux C |title=Identification of residues essential for catalysis and binding of calmodulin in rat brain inositol 1,4,5-trisphosphate 3-kinase. |journal=Biochem. J. |volume=280 ( Pt 1) |issue= |pages= 125-9 |year= 1992 |pmid= 1660262 |doi= }}
*{{cite journal  |vauthors=Takazawa K, Perret J, Dumont JE, Erneux C |title=Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase |journal=Biochem. Biophys. Res. Commun. |volume=174 |issue= 2 |pages= 529–35 |year= 1991 |pmid= 1847047 |doi=10.1016/0006-291X(91)91449-M  }}
*{{cite journal  | author=Takazawa K, Perret J, Dumont JE, Erneux C |title=Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase. |journal=Biochem. Biophys. Res. Commun. |volume=174 |issue= 2 |pages= 529-35 |year= 1991 |pmid= 1847047 |doi=  }}
*{{cite journal  |vauthors=Lin AN, Barnes S, Wallace RW |title=Phosphorylation by protein kinase C inactivates an inositol 1,4,5-trisphosphate 3-kinase purified from human platelets |journal=Biochem. Biophys. Res. Commun. |volume=170 |issue= 3 |pages= 1371–6 |year= 1990 |pmid= 2167676 |doi=10.1016/0006-291X(90)90546-Y }}
*{{cite journal  | author=Lin AN, Barnes S, Wallace RW |title=Phosphorylation by protein kinase C inactivates an inositol 1,4,5-trisphosphate 3-kinase purified from human platelets. |journal=Biochem. Biophys. Res. Commun. |volume=170 |issue= 3 |pages= 1371-6 |year= 1990 |pmid= 2167676 |doi=  }}
*{{cite journal  |vauthors=Takazawa K, Vandekerckhove J, Dumont JE, Erneux C |title=Cloning and expression in Escherichia coli of a rat brain cDNA encoding a Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase |journal=Biochem. J. |volume=272 |issue= 1 |pages= 107–12 |year= 1991 |pmid= 2176078 |doi= | pmc=1149663 }}
*{{cite journal  | author=Takazawa K, Perret J, Dumont JE, Erneux C |title=Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence. |journal=Nucleic Acids Res. |volume=18 |issue= 23 |pages= 7141 |year= 1991 |pmid= 2175886 |doi=  }}
*{{cite journal  |vauthors=Ryu SH, Lee SY, Lee KY, Rhee SG |title=Catalytic properties of inositol trisphosphate kinase: activation by Ca2+ and calmodulin |journal=FASEB J. |volume=1 |issue= 5 |pages= 388–93 |year= 1987 |pmid= 2824270 |doi=  }}
*{{cite journal  | author=Takazawa K, Vandekerckhove J, Dumont JE, Erneux C |title=Cloning and expression in Escherichia coli of a rat brain cDNA encoding a Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase. |journal=Biochem. J. |volume=272 |issue= 1 |pages= 107-12 |year= 1991 |pmid= 2176078 |doi=  }}
*{{cite journal  |vauthors=Communi D, Vanweyenberg V, Erneux C |title=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 |journal=EMBO J. |volume=16 |issue= 8 |pages= 1943–52 |year= 1997 |pmid= 9155020 |doi= 10.1093/emboj/16.8.1943 | pmc=1169797 }}
*{{cite journal  | author=Ryu SH, Lee SY, Lee KY, Rhee SG |title=Catalytic properties of inositol trisphosphate kinase: activation by Ca2+ and calmodulin. |journal=FASEB J. |volume=1 |issue= 5 |pages= 388-93 |year= 1987 |pmid= 2824270 |doi= }}
*{{cite journal  |vauthors=Woodring PJ, Garrison JC |title=Expression, purification, and regulation of two isoforms of the inositol 1,4,5-trisphosphate 3-kinase |journal=J. Biol. Chem. |volume=272 |issue= 48 |pages= 30447–54 |year= 1997 |pmid= 9374536 |doi=10.1074/jbc.272.48.30447  }}
*{{cite journal  | author=Communi D, Vanweyenberg V, Erneux C |title=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. |journal=EMBO J. |volume=16 |issue= 8 |pages= 1943-52 |year= 1997 |pmid= 9155020 |doi= 10.1093/emboj/16.8.1943 }}
*{{cite journal  |vauthors=Schell MJ, Erneux C, Irvine RF |title=Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus |journal=J. Biol. Chem. |volume=276 |issue= 40 |pages= 37537–46 |year= 2001 |pmid= 11468283 |doi= 10.1074/jbc.M104101200 }}
*{{cite journal  | author=Woodring PJ, Garrison JC |title=Expression, purification, and regulation of two isoforms of the inositol 1,4,5-trisphosphate 3-kinase. |journal=J. Biol. Chem. |volume=272 |issue= 48 |pages= 30447-54 |year= 1997 |pmid= 9374536 |doi=  }}
*{{cite journal  |vauthors=Mishra J, Bhalla US |title=Simulations of inositol phosphate metabolism and its interaction with InsP(3)-mediated calcium release |journal=Biophys. J. |volume=83 |issue= 3 |pages= 1298–316 |year= 2003 |pmid= 12202356 |doi=10.1016/S0006-3495(02)73901-5 | pmc=1302229  }}
*{{cite journal  | author=Schell MJ, Erneux C, Irvine RF |title=Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus. |journal=J. Biol. Chem. |volume=276 |issue= 40 |pages= 37537-46 |year= 2001 |pmid= 11468283 |doi= 10.1074/jbc.M104101200 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins | first6=FS | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal | author=Mishra J, Bhalla US |title=Simulations of inositol phosphate metabolism and its interaction with InsP(3)-mediated calcium release. |journal=Biophys. J. |volume=83 |issue= 3 |pages= 1298-316 |year= 2003 |pmid= 12202356 |doi=  }}
*{{cite journal  | author=Dewaste V |title=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 |journal=Biochem. J. |volume=374 |issue= Pt 1 |pages= 41–9 |year= 2003 |pmid= 12747803 |doi= 10.1042/BJ20021963  | pmc=1223573  |name-list-format=vanc| author2=Moreau C  | author3=De Smedt F  | display-authors=3 | last4=Bex  | first4=Françoise  | last5=De Smedt  | first5=Humbert  | last6=Wuytack  | first6=Frank  | last7=Missiaen  | first7=Ludwig  | last8=Erneux  | first8=Christophe }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=González B |title=Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase |journal=Mol. Cell |volume=15 |issue= 5 |pages= 689–701 |year= 2004 |pmid= 15350214 |doi= 10.1016/j.molcel.2004.08.004  |name-list-format=vanc| author2=Schell MJ  | author3=Letcher AJ  | display-authors=3  | last4=Veprintsev  | first4=Dmitry B.  | last5=Irvine  | first5=Robin F.  | last6=Williams  | first6=Roger L. }}
*{{cite journal  | author=Dewaste V, Moreau C, De Smedt F, ''et al.'' |title=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. |journal=Biochem. J. |volume=374 |issue= Pt 1 |pages= 41-9 |year= 2003 |pmid= 12747803 |doi= 10.1042/BJ20021963 }}
*{{cite journal  | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=González B, Schell MJ, Letcher AJ, ''et al.'' |title=Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase. |journal=Mol. Cell |volume=15 |issue= 5 |pages= 689-701 |year= 2004 |pmid= 15350214 |doi= 10.1016/j.molcel.2004.08.004 }}
*{{cite journal  | author=Kato H |title=Down-regulation of 1D-myo-inositol 1,4,5-trisphosphate 3-kinase A protein expression in oral squamous cell carcinoma |journal=Int. J. Oncol. |volume=28 |issue= 4 |pages= 873–81 |year= 2006 |pmid= 16525636 |doi=  10.3892/ijo.28.4.873|name-list-format=vanc| author2=Uzawa K  | author3=Onda T  | display-authors=3  | last4=Kato  | first4=Y  | last5=Saito  | first5=K  | last6=Nakashima  | first6=D  | last7=Ogawara  | first7=K  | last8=Bukawa  | first8=H  | last9=Yokoe  | first9=H }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Kato H, Uzawa K, Onda T, ''et al.'' |title=Down-regulation of 1D-myo-inositol 1,4,5-trisphosphate 3-kinase A protein expression in oral squamous cell carcinoma. |journal=Int. J. Oncol. |volume=28 |issue= 4 |pages= 873-81 |year= 2006 |pmid= 16525636 |doi=  }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3706}}
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Revision as of 00:13, 1 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Inositol-trisphosphate 3-kinase A is an enzyme that in humans is encoded by the ITPKA gene.[1][2][3]

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.[3]

References

  1. ↑ Erneux C, Roeckel N, Takazawa K, Mailleux P, Vassart G, Mattei MG (Dec 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. doi:10.1016/S0888-7543(05)80265-4. PMID 1330886.
  2. ↑ Takazawa K, Perret J, Dumont JE, Erneux C (Feb 1991). "Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence". Nucleic Acids Res. 18 (23): 7141. doi:10.1093/nar/18.23.7141. PMC 332787. PMID 2175886.
  3. ↑ 3.0 3.1 "Entrez Gene: ITPKA inositol 1,4,5-trisphosphate 3-kinase A".

Further reading



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